CA2205771C - Administration amelioree pour traitement de fond - Google Patents

Administration amelioree pour traitement de fond Download PDF

Info

Publication number: CA2205771C
Authority: CA; Canada
Prior art keywords: hyaluronan; hbm; amino acids; protein; basic amino
Prior art date: 1997-05-22
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Expired - Fee Related

Application number

CA002205771A

Other languages

English (en)

Other versions

CA2205771A1 (fr

Inventor

Eva A. Turley

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Jagotec AG

Original Assignee

Jagotec AG

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1997-05-22

Filing date

1997-05-22

Publication date

2002-05-14

1997-05-22 Application filed by Jagotec AG filed Critical Jagotec AG

1997-05-22 Priority to CA002205771A priority Critical patent/CA2205771C/fr

1998-05-11 Priority to NZ501270A priority patent/NZ501270A/en

1998-05-11 Priority to PCT/CA1998/000448 priority patent/WO1998052590A2/fr

1998-05-11 Priority to EP98920426A priority patent/EP0998297A2/fr

1998-05-11 Priority to AU73286/98A priority patent/AU740631B2/en

1998-05-11 Priority to JP54972998A priority patent/JP2001526666A/ja

1998-11-22 Publication of CA2205771A1 publication Critical patent/CA2205771A1/fr

2002-05-14 Application granted granted Critical

2002-05-14 Publication of CA2205771C publication Critical patent/CA2205771C/fr

2017-05-22 Anticipated expiration legal-status Critical

Status Expired - Fee Related legal-status Critical Current

Links

208000037265 diseases, disorders, signs and symptoms Diseases 0.000 title claims abstract description 59
201000010099 disease Diseases 0.000 title claims abstract description 57
239000003607 modifier Substances 0.000 title claims abstract description 45
229920002674 hyaluronan Polymers 0.000 claims abstract description 193
229940099552 hyaluronan Drugs 0.000 claims abstract description 157
KIUKXJAPPMFGSW-MNSSHETKSA-N hyaluronan Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)C1O[C@H]1[C@H](O)[C@@H](O)[C@H](O[C@H]2[C@@H](C(O[C@H]3[C@@H]([C@@H](O)[C@H](O)[C@H](O3)C(O)=O)O)[C@H](O)[C@@H](CO)O2)NC(C)=O)[C@@H](C(O)=O)O1 KIUKXJAPPMFGSW-MNSSHETKSA-N 0.000 claims abstract description 152
230000027455 binding Effects 0.000 claims abstract description 62
102000004169 proteins and genes Human genes 0.000 claims abstract description 55
108090000623 proteins and genes Proteins 0.000 claims abstract description 55
108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 42
239000008194 pharmaceutical composition Substances 0.000 claims abstract 17
150000001413 amino acids Chemical class 0.000 claims description 41
KIUKXJAPPMFGSW-DNGZLQJQSA-N (2S,3S,4S,5R,6R)-6-[(2S,3R,4R,5S,6R)-3-Acetamido-2-[(2S,3S,4R,5R,6R)-6-[(2R,3R,4R,5S,6R)-3-acetamido-2,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-2-carboxy-4,5-dihydroxyoxan-3-yl]oxy-5-hydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-3,4,5-trihydroxyoxane-2-carboxylic acid Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@H](O[C@H]2[C@@H]([C@@H](O[C@H]3[C@@H]([C@@H](O)[C@H](O)[C@H](O3)C(O)=O)O)[C@H](O)[C@@H](CO)O2)NC(C)=O)[C@@H](C(O)=O)O1 KIUKXJAPPMFGSW-DNGZLQJQSA-N 0.000 claims description 36
229960003160 hyaluronic acid Drugs 0.000 claims description 36
102000004127 Cytokines Human genes 0.000 claims description 23
108090000695 Cytokines Proteins 0.000 claims description 23
229920002385 Sodium hyaluronate Polymers 0.000 claims description 14
229940010747 sodium hyaluronate Drugs 0.000 claims description 14
YWIVKILSMZOHHF-QJZPQSOGSA-N sodium;(2s,3s,4s,5r,6r)-6-[(2s,3r,4r,5s,6r)-3-acetamido-2-[(2s,3s,4r,5r,6r)-6-[(2r,3r,4r,5s,6r)-3-acetamido-2,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-2-carboxy-4,5-dihydroxyoxan-3-yl]oxy-5-hydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-3,4,5-trihydroxyoxane-2- Chemical compound [Na+].CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@H](O[C@H]2[C@@H]([C@@H](O[C@H]3[C@@H]([C@@H](O)[C@H](O)[C@H](O3)C(O)=O)O)[C@H](O)[C@@H](CO)O2)NC(C)=O)[C@@H](C(O)=O)O1 YWIVKILSMZOHHF-QJZPQSOGSA-N 0.000 claims description 14
150000003839 salts Chemical class 0.000 claims description 13
230000002209 hydrophobic effect Effects 0.000 claims description 9
238000004519 manufacturing process Methods 0.000 claims description 7
102000035195 Peptidases Human genes 0.000 claims description 4
108091005804 Peptidases Proteins 0.000 claims description 4
239000004365 Protease Substances 0.000 claims description 4
210000000987 immune system Anatomy 0.000 claims description 2
239000000546 pharmaceutical excipient Substances 0.000 claims 2
229940124531 pharmaceutical excipient Drugs 0.000 claims 2
235000018102 proteins Nutrition 0.000 description 40
235000001014 amino acid Nutrition 0.000 description 23
238000000034 method Methods 0.000 description 19
102000004196 processed proteins & peptides Human genes 0.000 description 19
238000001990 intravenous administration Methods 0.000 description 18
239000003814 drug Substances 0.000 description 17
230000035772 mutation Effects 0.000 description 17
102000037865 fusion proteins Human genes 0.000 description 13
108020001507 fusion proteins Proteins 0.000 description 13
230000002434 immunopotentiative effect Effects 0.000 description 11
102000005962 receptors Human genes 0.000 description 11
108010013214 Hyaluronan Receptors Proteins 0.000 description 10
239000000427 antigen Substances 0.000 description 10
102000036639 antigens Human genes 0.000 description 10
108091007433 antigens Proteins 0.000 description 10
229940088597 hormone Drugs 0.000 description 10
239000005556 hormone Substances 0.000 description 10
238000012360 testing method Methods 0.000 description 10
CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 9
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 9
WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 9
239000002299 complementary DNA Substances 0.000 description 9
239000012634 fragment Substances 0.000 description 9
108020003175 receptors Proteins 0.000 description 9
102000018866 Hyaluronan Receptors Human genes 0.000 description 8
206010061218 Inflammation Diseases 0.000 description 8
XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 8
238000003556 assay Methods 0.000 description 8
230000004054 inflammatory process Effects 0.000 description 8
238000002347 injection Methods 0.000 description 8
239000007924 injection Substances 0.000 description 8
239000000047 product Substances 0.000 description 8
239000000243 solution Substances 0.000 description 8
230000001225 therapeutic effect Effects 0.000 description 8
210000001519 tissue Anatomy 0.000 description 8
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 8
102100032912 CD44 antigen Human genes 0.000 description 7
101000868273 Homo sapiens CD44 antigen Proteins 0.000 description 7
230000012010 growth Effects 0.000 description 7
230000000699 topical effect Effects 0.000 description 7
108020004635 Complementary DNA Proteins 0.000 description 6
206010020772 Hypertension Diseases 0.000 description 6
208000027418 Wounds and injury Diseases 0.000 description 6
230000006378 damage Effects 0.000 description 6
229940079593 drug Drugs 0.000 description 6
230000000694 effects Effects 0.000 description 6
208000014674 injury Diseases 0.000 description 6
238000007918 intramuscular administration Methods 0.000 description 6
230000002829 reductive effect Effects 0.000 description 6
229940124597 therapeutic agent Drugs 0.000 description 6
102000014914 Carrier Proteins Human genes 0.000 description 5
102000000844 Cell Surface Receptors Human genes 0.000 description 5
108010001857 Cell Surface Receptors Proteins 0.000 description 5
-1 IZHAMM Proteins 0.000 description 5
206010028980 Neoplasm Diseases 0.000 description 5
229920002684 Sepharose Polymers 0.000 description 5
108091008324 binding proteins Proteins 0.000 description 5
239000002158 endotoxin Substances 0.000 description 5
239000000499 gel Substances 0.000 description 5
229910001385 heavy metal Inorganic materials 0.000 description 5
108010003425 hyaluronan-mediated motility receptor Proteins 0.000 description 5
239000003112 inhibitor Substances 0.000 description 5
108700041430 link Proteins 0.000 description 5
244000005700 microbiome Species 0.000 description 5
239000000203 mixture Substances 0.000 description 5
201000006938 muscular dystrophy Diseases 0.000 description 5
239000000843 powder Substances 0.000 description 5
238000011282 treatment Methods 0.000 description 5
YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 4
229920001287 Chondroitin sulfate Polymers 0.000 description 4
229920002683 Glycosaminoglycan Polymers 0.000 description 4
241001529936 Murinae Species 0.000 description 4
240000004808 Saccharomyces cerevisiae Species 0.000 description 4
239000003242 anti bacterial agent Substances 0.000 description 4
229940088710 antibiotic agent Drugs 0.000 description 4
229910052785 arsenic Inorganic materials 0.000 description 4
RQNWIZPPADIBDY-UHFFFAOYSA-N arsenic atom Chemical compound [As] RQNWIZPPADIBDY-UHFFFAOYSA-N 0.000 description 4
230000008033 biological extinction Effects 0.000 description 4
125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 4
210000004027 cell Anatomy 0.000 description 4
230000007812 deficiency Effects 0.000 description 4
238000001035 drying Methods 0.000 description 4
RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 4
239000008187 granular material Substances 0.000 description 4
NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 4
229910052742 iron Inorganic materials 0.000 description 4
230000000813 microbial effect Effects 0.000 description 4
239000000137 peptide hydrolase inhibitor Substances 0.000 description 4
210000003491 skin Anatomy 0.000 description 4
238000007920 subcutaneous administration Methods 0.000 description 4
MOBOUQJWGBVNCR-NQYJQULFSA-N sulfazecin Chemical compound OC(=O)[C@H](N)CCC(=O)N[C@H](C)C(=O)N[C@@]1(OC)CN(S(O)(=O)=O)C1=O MOBOUQJWGBVNCR-NQYJQULFSA-N 0.000 description 4
101800000414 Corticotropin Proteins 0.000 description 3
239000000055 Corticotropin-Releasing Hormone Substances 0.000 description 3
241000588724 Escherichia coli Species 0.000 description 3
102100023122 Glycylpeptide N-tetradecanoyltransferase 2 Human genes 0.000 description 3
101710081889 Glycylpeptide N-tetradecanoyltransferase 2 Proteins 0.000 description 3
108010026389 Gramicidin Proteins 0.000 description 3
KJURKGLESSCVCL-UHFFFAOYSA-N Isosulfazecin Natural products COC1(CN(C1=O)S(=O)(=O)O)NC(=O)C(N)CC(=O)CCC(N)C(=O)O KJURKGLESSCVCL-UHFFFAOYSA-N 0.000 description 3
OVRNDRQMDRJTHS-UHFFFAOYSA-N N-acelyl-D-glucosamine Natural products CC(=O)NC1C(O)OC(CO)C(O)C1O OVRNDRQMDRJTHS-UHFFFAOYSA-N 0.000 description 3
OVRNDRQMDRJTHS-FMDGEEDCSA-N N-acetyl-beta-D-glucosamine Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-FMDGEEDCSA-N 0.000 description 3
MBLBDJOUHNCFQT-LXGUWJNJSA-N N-acetylglucosamine Natural products CC(=O)N[C@@H](C=O)[C@@H](O)[C@H](O)[C@H](O)CO MBLBDJOUHNCFQT-LXGUWJNJSA-N 0.000 description 3
108091034117 Oligonucleotide Proteins 0.000 description 3
229920002230 Pectic acid Polymers 0.000 description 3
102000009618 Transforming Growth Factors Human genes 0.000 description 3
108010009583 Transforming Growth Factors Proteins 0.000 description 3
108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 3
102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 3
108010059993 Vancomycin Proteins 0.000 description 3
JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 3
230000002378 acidificating effect Effects 0.000 description 3
238000000246 agarose gel electrophoresis Methods 0.000 description 3
230000036592 analgesia Effects 0.000 description 3
208000007502 anemia Diseases 0.000 description 3
230000001580 bacterial effect Effects 0.000 description 3
MSWZFWKMSRAUBD-UHFFFAOYSA-N beta-D-galactosamine Natural products NC1C(O)OC(CO)C(O)C1O MSWZFWKMSRAUBD-UHFFFAOYSA-N 0.000 description 3
238000002512 chemotherapy Methods 0.000 description 3
229940059329 chondroitin sulfate Drugs 0.000 description 3
238000010276 construction Methods 0.000 description 3
229960000258 corticotropin Drugs 0.000 description 3
IDLFZVILOHSSID-OVLDLUHVSA-N corticotropin Chemical compound C([C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(N)=O)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)NC(=O)[C@@H](N)CO)C1=CC=C(O)C=C1 IDLFZVILOHSSID-OVLDLUHVSA-N 0.000 description 3
230000029087 digestion Effects 0.000 description 3
238000002474 experimental method Methods 0.000 description 3
230000004720 fertilization Effects 0.000 description 3
230000002496 gastric effect Effects 0.000 description 3
229940097043 glucuronic acid Drugs 0.000 description 3
230000006698 induction Effects 0.000 description 3
208000000509 infertility Diseases 0.000 description 3
230000036512 infertility Effects 0.000 description 3
238000002329 infrared spectrum Methods 0.000 description 3
210000004185 liver Anatomy 0.000 description 3
230000003211 malignant effect Effects 0.000 description 3
229950006780 n-acetylglucosamine Drugs 0.000 description 3
230000001575 pathological effect Effects 0.000 description 3
239000010318 polygalacturonic acid Substances 0.000 description 3
230000008569 process Effects 0.000 description 3
XNSAINXGIQZQOO-SRVKXCTJSA-N protirelin Chemical compound NC(=O)[C@@H]1CCCN1C(=O)[C@@H](NC(=O)[C@H]1NC(=O)CC1)CC1=CN=CN1 XNSAINXGIQZQOO-SRVKXCTJSA-N 0.000 description 3
239000003488 releasing hormone Substances 0.000 description 3
239000013557 residual solvent Substances 0.000 description 3
159000000000 sodium salts Chemical group 0.000 description 3
238000001228 spectrum Methods 0.000 description 3
239000008223 sterile water Substances 0.000 description 3
230000004936 stimulating effect Effects 0.000 description 3
239000000126 substance Substances 0.000 description 3
230000008685 targeting Effects 0.000 description 3
231100000419 toxicity Toxicity 0.000 description 3
230000001988 toxicity Effects 0.000 description 3
229960003165 vancomycin Drugs 0.000 description 3
MYPYJXKWCTUITO-LYRMYLQWSA-N vancomycin Chemical group O([C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1=C2C=C3C=C1OC1=CC=C(C=C1Cl)[C@@H](O)[C@H](C(N[C@@H](CC(N)=O)C(=O)N[C@H]3C(=O)N[C@H]1C(=O)N[C@H](C(N[C@@H](C3=CC(O)=CC(O)=C3C=3C(O)=CC=C1C=3)C(O)=O)=O)[C@H](O)C1=CC=C(C(=C1)Cl)O2)=O)NC(=O)[C@@H](CC(C)C)NC)[C@H]1C[C@](C)(N)[C@H](O)[C@H](C)O1 MYPYJXKWCTUITO-LYRMYLQWSA-N 0.000 description 3
MYPYJXKWCTUITO-UHFFFAOYSA-N vancomycin Natural products O1C(C(=C2)Cl)=CC=C2C(O)C(C(NC(C2=CC(O)=CC(O)=C2C=2C(O)=CC=C3C=2)C(O)=O)=O)NC(=O)C3NC(=O)C2NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(CC(C)C)NC)C(O)C(C=C3Cl)=CC=C3OC3=CC2=CC1=C3OC1OC(CO)C(O)C(O)C1OC1CC(C)(N)C(O)C(C)O1 MYPYJXKWCTUITO-UHFFFAOYSA-N 0.000 description 3
ZUEKKUYIXILDAF-WKEGUHRASA-N (2s)-2-[(4s)-4-acetamido-3-oxo-1,2-oxazolidin-2-yl]-5-oxooxolane-2-carboxylic acid Chemical compound O=C1[C@@H](NC(=O)C)CON1[C@]1(C(O)=O)OC(=O)CC1 ZUEKKUYIXILDAF-WKEGUHRASA-N 0.000 description 2
LLPMPMKLOHAIMY-QWRGUYRKSA-N (2s)-2-[2-[[(1s)-1-carboxy-2-(1h-imidazol-5-yl)ethyl]amino]ethylamino]-5-(diaminomethylideneamino)pentanoic acid Chemical compound NC(N)=NCCC[C@@H](C(O)=O)NCCN[C@H](C(O)=O)CC1=CN=CN1 LLPMPMKLOHAIMY-QWRGUYRKSA-N 0.000 description 2
LMDZBCPBFSXMTL-UHFFFAOYSA-N 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide Chemical compound CCN=C=NCCCN(C)C LMDZBCPBFSXMTL-UHFFFAOYSA-N 0.000 description 2
IQMHGRIOYXVPSE-UHFFFAOYSA-N 2-acetamido-5-[formyl(hydroxy)amino]-n-[1-[3-[5-[3-[formyl(hydroxy)amino]propyl]-3,6-dioxopiperazin-2-yl]propyl-hydroxyamino]-3-hydroxy-1-oxopropan-2-yl]pentanamide Chemical compound O=CN(O)CCCC(NC(=O)C)C(=O)NC(CO)C(=O)N(O)CCCC1NC(=O)C(CCCN(O)C=O)NC1=O IQMHGRIOYXVPSE-UHFFFAOYSA-N 0.000 description 2
MSWZFWKMSRAUBD-IVMDWMLBSA-N 2-amino-2-deoxy-D-glucopyranose Chemical compound N[C@H]1C(O)O[C@H](CO)[C@@H](O)[C@@H]1O MSWZFWKMSRAUBD-IVMDWMLBSA-N 0.000 description 2
SQDAZGGFXASXDW-UHFFFAOYSA-N 5-bromo-2-(trifluoromethoxy)pyridine Chemical compound FC(F)(F)OC1=CC=C(Br)C=N1 SQDAZGGFXASXDW-UHFFFAOYSA-N 0.000 description 2
239000005541 ACE inhibitor Substances 0.000 description 2
206010000599 Acromegaly Diseases 0.000 description 2
206010001928 Amenorrhoea Diseases 0.000 description 2
108010087765 Antipain Proteins 0.000 description 2
101710081722 Antitrypsin Proteins 0.000 description 2
IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
208000023275 Autoimmune disease Diseases 0.000 description 2
241000894006 Bacteria Species 0.000 description 2
208000035143 Bacterial infection Diseases 0.000 description 2
VGGGPCQERPFHOB-MCIONIFRSA-N Bestatin Chemical compound CC(C)C[C@H](C(O)=O)NC(=O)[C@@H](O)[C@H](N)CC1=CC=CC=C1 VGGGPCQERPFHOB-MCIONIFRSA-N 0.000 description 2
VGGGPCQERPFHOB-UHFFFAOYSA-N Bestatin Natural products CC(C)CC(C(O)=O)NC(=O)C(O)C(N)CC1=CC=CC=C1 VGGGPCQERPFHOB-UHFFFAOYSA-N 0.000 description 2
108091003079 Bovine Serum Albumin Proteins 0.000 description 2
102400000113 Calcitonin Human genes 0.000 description 2
108060001064 Calcitonin Proteins 0.000 description 2
208000005623 Carcinogenesis Diseases 0.000 description 2
BGRDGTOTEZBYJX-LNMVFDGZSA-N Cephabacin F3 Chemical compound S1CC(COC(=O)C[C@@H](O)[C@H](CCCN=C(N)N)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H](N)C)=C(C(O)=O)N2C(=O)[C@@](NC=O)(NC(=O)CCC[C@@H](N)C(O)=O)[C@@H]12 BGRDGTOTEZBYJX-LNMVFDGZSA-N 0.000 description 2
102000012289 Corticotropin-Releasing Hormone Human genes 0.000 description 2
108010022152 Corticotropin-Releasing Hormone Proteins 0.000 description 2
206010011498 Cryptorchism Diseases 0.000 description 2
108020004414 DNA Proteins 0.000 description 2
206010011985 Decubitus ulcer Diseases 0.000 description 2
102000003951 Erythropoietin Human genes 0.000 description 2
108090000394 Erythropoietin Proteins 0.000 description 2
108010037362 Extracellular Matrix Proteins Proteins 0.000 description 2
102000010834 Extracellular Matrix Proteins Human genes 0.000 description 2
102000012673 Follicle Stimulating Hormone Human genes 0.000 description 2
108010079345 Follicle Stimulating Hormone Proteins 0.000 description 2
IAJILQKETJEXLJ-UHFFFAOYSA-N Galacturonsaeure Natural products O=CC(O)C(O)C(O)C(O)C(O)=O IAJILQKETJEXLJ-UHFFFAOYSA-N 0.000 description 2
108010024636 Glutathione Proteins 0.000 description 2
108010086677 Gonadotropins Proteins 0.000 description 2
102000006771 Gonadotropins Human genes 0.000 description 2
HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 2
LLPMPMKLOHAIMY-UHFFFAOYSA-N Histargin Natural products NC(N)=NCCCC(C(O)=O)NCCNC(C(O)=O)CC1=CN=CN1 LLPMPMKLOHAIMY-UHFFFAOYSA-N 0.000 description 2
101001076292 Homo sapiens Insulin-like growth factor II Proteins 0.000 description 2
208000037147 Hypercalcaemia Diseases 0.000 description 2
102000004877 Insulin Human genes 0.000 description 2
108090001061 Insulin Proteins 0.000 description 2
102100025947 Insulin-like growth factor II Human genes 0.000 description 2
208000007766 Kaposi sarcoma Diseases 0.000 description 2
GOQOSUKANLZOQD-UHFFFAOYSA-N Lactivicin Natural products CC(=O)NC1CON(C2CC(=O)OC2C(=O)O)C1=O GOQOSUKANLZOQD-UHFFFAOYSA-N 0.000 description 2
GDBQQVLCIARPGH-UHFFFAOYSA-N Leupeptin Natural products CC(C)CC(NC(C)=O)C(=O)NC(CC(C)C)C(=O)NC(C=O)CCCN=C(N)N GDBQQVLCIARPGH-UHFFFAOYSA-N 0.000 description 2
102000007651 Macrophage Colony-Stimulating Factor Human genes 0.000 description 2
108010046938 Macrophage Colony-Stimulating Factor Proteins 0.000 description 2
102400001103 Neurotensin Human genes 0.000 description 2
101800001814 Neurotensin Proteins 0.000 description 2
208000001132 Osteoporosis Diseases 0.000 description 2
102400000050 Oxytocin Human genes 0.000 description 2
101800000989 Oxytocin Proteins 0.000 description 2
XNOPRXBHLZRZKH-UHFFFAOYSA-N Oxytocin Natural products N1C(=O)C(N)CSSCC(C(=O)N2C(CCC2)C(=O)NC(CC(C)C)C(=O)NCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(CCC(N)=O)NC(=O)C(C(C)CC)NC(=O)C1CC1=CC=C(O)C=C1 XNOPRXBHLZRZKH-UHFFFAOYSA-N 0.000 description 2
208000002193 Pain Diseases 0.000 description 2
108010081391 Ristocetin Proteins 0.000 description 2
108010071390 Serum Albumin Proteins 0.000 description 2
102000007562 Serum Albumin Human genes 0.000 description 2
108010023197 Streptokinase Proteins 0.000 description 2
108010053950 Teicoplanin Proteins 0.000 description 2
108010000499 Thromboplastin Proteins 0.000 description 2
102000002262 Thromboplastin Human genes 0.000 description 2
XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
FHIABUHDBXFQIT-JSNQUVIDSA-N actinoidin Chemical compound O1[C@@H](C)[C@H](OC)[C@@H](N)C[C@@H]1OC(C1C(NC(C2=CC(O)=CC(O[C@@H]3[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)O)=C2C=2C(O)=CC=C(C=2)C(NC(=O)C2NC(=O)C(CC=3C=CC=CC=3)NC(=O)C(NC(=O)C(N)C=3C=CC(O)=CC=3)C(O)C=3C=CC(O4)=CC=3)C(=O)N1)C(O)=O)=O)C(C=C1Cl)=CC=C1OC1=C(O[C@H]3[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)O[C@@H]3O[C@@H](C)[C@H](O)[C@@H](N)C3)C4=CC2=C1 FHIABUHDBXFQIT-JSNQUVIDSA-N 0.000 description 2
108700031667 actinoidins Proteins 0.000 description 2
208000017515 adrenocortical insufficiency Diseases 0.000 description 2
IAJILQKETJEXLJ-QTBDOELSSA-N aldehydo-D-glucuronic acid Chemical compound O=C[C@H](O)[C@@H](O)[C@H](O)[C@H](O)C(O)=O IAJILQKETJEXLJ-QTBDOELSSA-N 0.000 description 2
230000001475 anti-trypsic effect Effects 0.000 description 2
SDNYTAYICBFYFH-TUFLPTIASA-N antipain Chemical compound NC(N)=NCCC[C@@H](C=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 SDNYTAYICBFYFH-TUFLPTIASA-N 0.000 description 2
208000022362 bacterial infectious disease Diseases 0.000 description 2
230000015572 biosynthetic process Effects 0.000 description 2
229960002685 biotin Drugs 0.000 description 2
235000020958 biotin Nutrition 0.000 description 2
239000011616 biotin Substances 0.000 description 2
230000037396 body weight Effects 0.000 description 2
210000000988 bone and bone Anatomy 0.000 description 2
210000001185 bone marrow Anatomy 0.000 description 2
229940098773 bovine serum albumin Drugs 0.000 description 2
210000004899 c-terminal region Anatomy 0.000 description 2
229960004015 calcitonin Drugs 0.000 description 2
BBBFJLBPOGFECG-VJVYQDLKSA-N calcitonin Chemical compound N([C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(N)=O)C(C)C)C(=O)[C@@H]1CSSC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1 BBBFJLBPOGFECG-VJVYQDLKSA-N 0.000 description 2
230000036952 cancer formation Effects 0.000 description 2
239000004202 carbamide Substances 0.000 description 2
231100000504 carcinogenesis Toxicity 0.000 description 2
239000013592 cell lysate Substances 0.000 description 2
230000001413 cellular effect Effects 0.000 description 2
BGTFCAQCKWKTRL-YDEUACAXSA-N chembl1095986 Chemical compound C1[C@@H](N)[C@@H](O)[C@H](C)O[C@H]1O[C@@H]([C@H]1C(N[C@H](C2=CC(O)=CC(O[C@@H]3[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)O)=C2C=2C(O)=CC=C(C=2)[C@@H](NC(=O)[C@@H]2NC(=O)[C@@H]3C=4C=C(C(=C(O)C=4)C)OC=4C(O)=CC=C(C=4)[C@@H](N)C(=O)N[C@@H](C(=O)N3)[C@H](O)C=3C=CC(O4)=CC=3)C(=O)N1)C(O)=O)=O)C(C=C1)=CC=C1OC1=C(O[C@@H]3[C@H]([C@H](O)[C@@H](O)[C@H](CO[C@@H]5[C@H]([C@@H](O)[C@H](O)[C@@H](C)O5)O)O3)O[C@@H]3[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O3)O[C@@H]3[C@H]([C@H](O)[C@@H](CO)O3)O)C4=CC2=C1 BGTFCAQCKWKTRL-YDEUACAXSA-N 0.000 description 2
DDTDNCYHLGRFBM-YZEKDTGTSA-N chembl2367892 Chemical compound CC(=O)N[C@H]1[C@@H](O)[C@H](O)[C@H](CO)O[C@H]1O[C@@H]([C@H]1C(N[C@@H](C2=CC(O)=CC(O[C@@H]3[C@H]([C@H](O)[C@H](O)[C@@H](CO)O3)O)=C2C=2C(O)=CC=C(C=2)[C@@H](NC(=O)[C@@H]2NC(=O)[C@@H]3C=4C=C(O)C=C(C=4)OC=4C(O)=CC=C(C=4)[C@@H](N)C(=O)N[C@H](CC=4C=C(Cl)C(O5)=CC=4)C(=O)N3)C(=O)N1)C(O)=O)=O)C(C=C1Cl)=CC=C1OC1=C(O[C@H]3[C@H]([C@@H](O)[C@H](O)[C@H](CO)O3)NC(C)=O)C5=CC2=C1 DDTDNCYHLGRFBM-YZEKDTGTSA-N 0.000 description 2
238000006243 chemical reaction Methods 0.000 description 2
150000001875 compounds Chemical class 0.000 description 2
229940041967 corticotropin-releasing hormone Drugs 0.000 description 2
KLVRDXBAMSPYKH-RKYZNNDCSA-N corticotropin-releasing hormone (human) Chemical compound C([C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(N)=O)[C@@H](C)CC)NC(=O)[C@H](C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](C)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H]1N(CCC1)C(=O)[C@H]1N(CCC1)C(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](N)CO)[C@@H](C)CC)C(C)C)C(C)C)C1=CNC=N1 KLVRDXBAMSPYKH-RKYZNNDCSA-N 0.000 description 2
239000006071 cream Substances 0.000 description 2
201000000160 cryptorchidism Diseases 0.000 description 2
229930182912 cyclosporin Natural products 0.000 description 2
238000012217 deletion Methods 0.000 description 2
230000037430 deletion Effects 0.000 description 2
206010012601 diabetes mellitus Diseases 0.000 description 2
238000003745 diagnosis Methods 0.000 description 2
229940039227 diagnostic agent Drugs 0.000 description 2
239000000032 diagnostic agent Substances 0.000 description 2
208000035475 disorder Diseases 0.000 description 2
238000001962 electrophoresis Methods 0.000 description 2
210000002889 endothelial cell Anatomy 0.000 description 2
229940088598 enzyme Drugs 0.000 description 2
210000002744 extracellular matrix Anatomy 0.000 description 2
210000002950 fibroblast Anatomy 0.000 description 2
229940028334 follicle stimulating hormone Drugs 0.000 description 2
MWSKDGPKFCWPOF-UHFFFAOYSA-N forphenicine Chemical compound OC(=O)C(N)C1=CC=C(C=O)C(O)=C1 MWSKDGPKFCWPOF-UHFFFAOYSA-N 0.000 description 2
230000004927 fusion Effects 0.000 description 2
229960002442 glucosamine Drugs 0.000 description 2
229960003180 glutathione Drugs 0.000 description 2
239000002622 gonadotropin Substances 0.000 description 2
229960004905 gramicidin Drugs 0.000 description 2
ZWCXYZRRTRDGQE-SORVKSEFSA-N gramicidina Chemical compound C1=CC=C2C(C[C@H](NC(=O)[C@@H](CC(C)C)NC(=O)[C@H](CC=3C4=CC=CC=C4NC=3)NC(=O)[C@@H](CC(C)C)NC(=O)[C@H](CC=3C4=CC=CC=C4NC=3)NC(=O)[C@@H](CC(C)C)NC(=O)[C@H](CC=3C4=CC=CC=C4NC=3)NC(=O)[C@H](C(C)C)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](C(C)C)NC(=O)[C@H](C)NC(=O)[C@H](NC(=O)[C@H](C)NC(=O)CNC(=O)[C@@H](NC=O)C(C)C)CC(C)C)C(=O)NCCO)=CNC2=C1 ZWCXYZRRTRDGQE-SORVKSEFSA-N 0.000 description 2
230000005484 gravity Effects 0.000 description 2
239000003102 growth factor Substances 0.000 description 2
229920000669 heparin Polymers 0.000 description 2
229960002897 heparin Drugs 0.000 description 2
230000000148 hypercalcaemia Effects 0.000 description 2
208000030915 hypercalcemia disease Diseases 0.000 description 2
238000001727 in vivo Methods 0.000 description 2
208000021267 infertility disease Diseases 0.000 description 2
229940125396 insulin Drugs 0.000 description 2
229940068935 insulin-like growth factor 2 Drugs 0.000 description 2
108010082761 lactivicin Proteins 0.000 description 2
GDBQQVLCIARPGH-ULQDDVLXSA-N leupeptin Chemical compound CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C=O)CCCN=C(N)N GDBQQVLCIARPGH-ULQDDVLXSA-N 0.000 description 2
108010052968 leupeptin Proteins 0.000 description 2
239000007788 liquid Substances 0.000 description 2
239000006166 lysate Substances 0.000 description 2
239000000463 material Substances 0.000 description 2
210000002752 melanocyte Anatomy 0.000 description 2
BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 2
PCJGZPGTCUMMOT-ISULXFBGSA-N neurotensin Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCCCN)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]1NC(=O)CC1)C1=CC=C(O)C=C1 PCJGZPGTCUMMOT-ISULXFBGSA-N 0.000 description 2
239000002773 nucleotide Substances 0.000 description 2
125000003729 nucleotide group Chemical group 0.000 description 2
230000016087 ovulation Effects 0.000 description 2
XNOPRXBHLZRZKH-DSZYJQQASA-N oxytocin Chemical compound C([C@H]1C(=O)N[C@H](C(N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CSSC[C@H](N)C(=O)N1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(C)C)C(=O)NCC(N)=O)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 XNOPRXBHLZRZKH-DSZYJQQASA-N 0.000 description 2
229960001723 oxytocin Drugs 0.000 description 2
239000013618 particulate matter Substances 0.000 description 2
125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
238000000159 protein binding assay Methods 0.000 description 2
238000010188 recombinant method Methods 0.000 description 2
238000011084 recovery Methods 0.000 description 2
230000001105 regulatory effect Effects 0.000 description 2
108091008146 restriction endonucleases Proteins 0.000 description 2
229950004257 ristocetin Drugs 0.000 description 2
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
229960005202 streptokinase Drugs 0.000 description 2
229960001608 teicoplanin Drugs 0.000 description 2
210000001685 thyroid gland Anatomy 0.000 description 2
239000002753 trypsin inhibitor Substances 0.000 description 2
229950009811 ubenimex Drugs 0.000 description 2
229960005356 urokinase Drugs 0.000 description 2
210000004127 vitreous body Anatomy 0.000 description 2
MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
MOBOUQJWGBVNCR-QRPMWFLTSA-N (2r)-2-amino-5-[[(2s)-1-[[(3r)-3-methoxy-2-oxo-1-sulfoazetidin-3-yl]amino]-1-oxopropan-2-yl]amino]-5-oxopentanoic acid Chemical compound OC(=O)[C@H](N)CCC(=O)N[C@@H](C)C(=O)N[C@@]1(OC)CN(S(O)(=O)=O)C1=O MOBOUQJWGBVNCR-QRPMWFLTSA-N 0.000 description 1
WZFDNGAENBEYMA-GXSJLCMTSA-N (2r,3s)-3-amino-2-hydroxy-2-(1h-imidazol-5-ylmethyl)-5-methylhexanoic acid Chemical compound CC(C)C[C@H](N)[C@@](O)(C(O)=O)CC1=CN=CN1 WZFDNGAENBEYMA-GXSJLCMTSA-N 0.000 description 1
CEQMEILRVSCKGT-FXTUREPZSA-N (2s)-1-[(2s)-1-[(2s)-2-[[(2s,3r)-3-amino-2-hydroxy-4-phenylbutanoyl]amino]-4-methylpentanoyl]pyrrolidine-2-carbonyl]pyrrolidine-2-carboxylic acid Chemical compound C([C@@H](N)[C@H](O)C(=O)N[C@@H](CC(C)C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(O)=O)C1=CC=CC=C1 CEQMEILRVSCKGT-FXTUREPZSA-N 0.000 description 1
VKZRWSNIWNFCIQ-WDSKDSINSA-N (2s)-2-[2-[[(1s)-1,2-dicarboxyethyl]amino]ethylamino]butanedioic acid Chemical compound OC(=O)C[C@@H](C(O)=O)NCCN[C@H](C(O)=O)CC(O)=O VKZRWSNIWNFCIQ-WDSKDSINSA-N 0.000 description 1
MRXDGVXSWIXTQL-HYHFHBMOSA-N (2s)-2-[[(1s)-1-(2-amino-1,4,5,6-tetrahydropyrimidin-6-yl)-2-[[(2s)-4-methyl-1-oxo-1-[[(2s)-1-oxo-3-phenylpropan-2-yl]amino]pentan-2-yl]amino]-2-oxoethyl]carbamoylamino]-3-phenylpropanoic acid Chemical compound C([C@H](NC(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C=O)C1NC(N)=NCC1)C(O)=O)C1=CC=CC=C1 MRXDGVXSWIXTQL-HYHFHBMOSA-N 0.000 description 1
IJWCGVPEDDQUDE-YGJAXBLXSA-N (2s)-2-[[(1s)-2-[[(2s)-5-amino-1,5-dioxo-1-[[(2s)-1-oxopropan-2-yl]amino]pentan-2-yl]amino]-1-[(6s)-2-amino-1,4,5,6-tetrahydropyrimidin-6-yl]-2-oxoethyl]carbamoylamino]-4-methylpentanoic acid Chemical compound O=C[C@H](C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)N[C@@H](CC(C)C)C(O)=O)[C@@H]1CCN=C(N)N1 IJWCGVPEDDQUDE-YGJAXBLXSA-N 0.000 description 1
UNPBSZUDTFBULK-CZCKBYKRSA-N (2s)-2-[[(2r)-2-[[(3s)-3-amino-2-oxopentanoyl]amino]-4-methylpentanoyl]-[(2s,6s)-2,6-diamino-3,7-dimethyl-5-oxooctanoyl]amino]-3-methylbutanoic acid Chemical compound CC[C@H](N)C(=O)C(=O)N[C@H](CC(C)C)C(=O)N([C@@H](C(C)C)C(O)=O)C(=O)[C@@H](N)C(C)CC(=O)[C@@H](N)C(C)C UNPBSZUDTFBULK-CZCKBYKRSA-N 0.000 description 1
ZMEWRPBAQVSBBB-GOTSBHOMSA-N (2s)-2-[[(2s)-2-[(2-aminoacetyl)amino]-3-(4-hydroxyphenyl)propanoyl]amino]-6-[[2-[2-[2-[bis(carboxymethyl)amino]ethyl-(carboxymethyl)amino]ethyl-(carboxymethyl)amino]acetyl]amino]hexanoic acid Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CCN(CC(O)=O)CC(=O)NCCCC[C@@H](C(O)=O)NC(=O)[C@@H](NC(=O)CN)CC1=CC=C(O)C=C1 ZMEWRPBAQVSBBB-GOTSBHOMSA-N 0.000 description 1
ZRZROXNBKJAOKB-GFVHOAGBSA-N (2s)-2-[[2-[[(2s)-2-[[(2s)-2-[[(2s)-2-[[2-[[2-[[(2s)-2-[[(2s)-2-amino-3-(1h-indol-3-yl)propanoyl]amino]propanoyl]amino]acetyl]amino]acetyl]amino]-3-carboxypropanoyl]amino]propanoyl]amino]-3-hydroxypropanoyl]amino]acetyl]amino]pentanedioic acid Chemical compound C1=CC=C2C(C[C@H](N)C(=O)N[C@@H](C)C(=O)NCC(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(O)=O)=CNC2=C1 ZRZROXNBKJAOKB-GFVHOAGBSA-N 0.000 description 1
JRBXPUUAYKCCLQ-QMMMGPOBSA-N (2s)-2-amino-2-[3-hydroxy-4-(hydroxymethyl)phenyl]acetic acid Chemical compound OC(=O)[C@@H](N)C1=CC=C(CO)C(O)=C1 JRBXPUUAYKCCLQ-QMMMGPOBSA-N 0.000 description 1
ZNAJIKYTBCGAQQ-NSHDSACASA-N (2s)-2-benzyl-2-hydroxybutanedioic acid Chemical compound OC(=O)C[C@](O)(C(O)=O)CC1=CC=CC=C1 ZNAJIKYTBCGAQQ-NSHDSACASA-N 0.000 description 1
RDGABBULIYLDER-NWCZBACYSA-N (3s)-4-[[(2s)-2-[[(3s,4s)-4-[[(2s,6s)-1-amino-3,7-dimethyl-6-(3-methylbutanoylamino)-1,5-dioxooctan-2-yl]amino]-3-hydroxy-6-methylheptanoyl]amino]-3-hydroxypropanoyl]amino]-3-hydroxy-6-methylheptanoic acid Chemical compound CC(C)CC(=O)N[C@@H](C(C)C)C(=O)CC(C)[C@@H](C(N)=O)N[C@@H](CC(C)C)[C@@H](O)CC(=O)N[C@@H](CO)C(=O)NC(CC(C)C)[C@@H](O)CC(O)=O RDGABBULIYLDER-NWCZBACYSA-N 0.000 description 1
DEQANNDTNATYII-OULOTJBUSA-N (4r,7s,10s,13r,16s,19r)-10-(4-aminobutyl)-19-[[(2r)-2-amino-3-phenylpropanoyl]amino]-16-benzyl-n-[(2r,3r)-1,3-dihydroxybutan-2-yl]-7-[(1r)-1-hydroxyethyl]-13-(1h-indol-3-ylmethyl)-6,9,12,15,18-pentaoxo-1,2-dithia-5,8,11,14,17-pentazacycloicosane-4-carboxa Chemical compound C([C@@H](N)C(=O)N[C@H]1CSSC[C@H](NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](CC=2C3=CC=CC=C3NC=2)NC(=O)[C@H](CC=2C=CC=CC=2)NC1=O)C(=O)N[C@H](CO)[C@H](O)C)C1=CC=CC=C1 DEQANNDTNATYII-OULOTJBUSA-N 0.000 description 1
108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
QRBLKGHRWFGINE-UGWAGOLRSA-N 2-[2-[2-[[2-[[4-[[2-[[6-amino-2-[3-amino-1-[(2,3-diamino-3-oxopropyl)amino]-3-oxopropyl]-5-methylpyrimidine-4-carbonyl]amino]-3-[(2r,3s,4s,5s,6s)-3-[(2s,3r,4r,5s)-4-carbamoyl-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-4,5-dihydroxy-6-(hydroxymethyl)- Chemical compound N=1C(C=2SC=C(N=2)C(N)=O)CSC=1CCNC(=O)C(C(C)=O)NC(=O)C(C)C(O)C(C)NC(=O)C(C(O[C@H]1[C@@]([C@@H](O)[C@H](O)[C@H](CO)O1)(C)O[C@H]1[C@@H]([C@](O)([C@@H](O)C(CO)O1)C(N)=O)O)C=1NC=NC=1)NC(=O)C1=NC(C(CC(N)=O)NCC(N)C(N)=O)=NC(N)=C1C QRBLKGHRWFGINE-UGWAGOLRSA-N 0.000 description 1
OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 1
UDZMHVWZLRBHMW-UHFFFAOYSA-N 4-(4-aminophenyl)aniline;periodic acid Chemical compound OI(=O)(=O)=O.C1=CC(N)=CC=C1C1=CC=C(N)C=C1 UDZMHVWZLRBHMW-UHFFFAOYSA-N 0.000 description 1
102100031585 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 Human genes 0.000 description 1
208000030507 AIDS Diseases 0.000 description 1
QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
208000024893 Acute lymphoblastic leukemia Diseases 0.000 description 1
208000014697 Acute lymphocytic leukaemia Diseases 0.000 description 1
239000000275 Adrenocorticotropic Hormone Substances 0.000 description 1
102100036601 Aggrecan core protein Human genes 0.000 description 1
108010067219 Aggrecans Proteins 0.000 description 1
108010088751 Albumins Proteins 0.000 description 1
102000009027 Albumins Human genes 0.000 description 1
201000000736 Amenorrhea Diseases 0.000 description 1
102000004400 Aminopeptidases Human genes 0.000 description 1
108090000915 Aminopeptidases Proteins 0.000 description 1
VHUUQVKOLVNVRT-UHFFFAOYSA-N Ammonium hydroxide Chemical compound [NH4+].[OH-] VHUUQVKOLVNVRT-UHFFFAOYSA-N 0.000 description 1
102100022987 Angiogenin Human genes 0.000 description 1
206010059313 Anogenital warts Diseases 0.000 description 1
102000044503 Antimicrobial Peptides Human genes 0.000 description 1
108700042778 Antimicrobial Peptides Proteins 0.000 description 1
102000004411 Antithrombin III Human genes 0.000 description 1
108090000935 Antithrombin III Proteins 0.000 description 1
108010039627 Aprotinin Proteins 0.000 description 1
239000004475 Arginine Substances 0.000 description 1
229930184223 Arphamenine Natural products 0.000 description 1
206010003445 Ascites Diseases 0.000 description 1
102000015790 Asparaginase Human genes 0.000 description 1
108010024976 Asparaginase Proteins 0.000 description 1
239000004184 Avoparcin Substances 0.000 description 1
108010001478 Bacitracin Proteins 0.000 description 1
108010006654 Bleomycin Proteins 0.000 description 1
BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
241000283690 Bos taurus Species 0.000 description 1
206010058019 Cancer Pain Diseases 0.000 description 1
102000005367 Carboxypeptidases Human genes 0.000 description 1
108010006303 Carboxypeptidases Proteins 0.000 description 1
229930191274 Chitinovorin Natural products 0.000 description 1
101800001982 Cholecystokinin Proteins 0.000 description 1
102100025841 Cholecystokinin Human genes 0.000 description 1
208000000668 Chronic Pancreatitis Diseases 0.000 description 1
OLVPQBGMUGIKIW-UHFFFAOYSA-N Chymostatin Natural products C=1C=CC=CC=1CC(C=O)NC(=O)C(C(C)CC)NC(=O)C(C1NC(N)=NCC1)NC(=O)NC(C(O)=O)CC1=CC=CC=C1 OLVPQBGMUGIKIW-UHFFFAOYSA-N 0.000 description 1
102000005853 Clathrin Human genes 0.000 description 1
108010019874 Clathrin Proteins 0.000 description 1
241000190137 Clathrinida Species 0.000 description 1
102100022641 Coagulation factor IX Human genes 0.000 description 1
102100023804 Coagulation factor VII Human genes 0.000 description 1
108020004705 Codon Proteins 0.000 description 1
108010035532 Collagen Proteins 0.000 description 1
102000008186 Collagen Human genes 0.000 description 1
208000029147 Collagen-vascular disease Diseases 0.000 description 1
208000001333 Colorectal Neoplasms Diseases 0.000 description 1
208000000907 Condylomata Acuminata Diseases 0.000 description 1
206010010356 Congenital anomaly Diseases 0.000 description 1
102400000739 Corticotropin Human genes 0.000 description 1
108010091893 Cosyntropin Proteins 0.000 description 1
108010069514 Cyclic Peptides Proteins 0.000 description 1
102000001189 Cyclic Peptides Human genes 0.000 description 1
PMATZTZNYRCHOR-CGLBZJNRSA-N Cyclosporin A Chemical compound CC[C@@H]1NC(=O)[C@H]([C@H](O)[C@H](C)C\C=C\C)N(C)C(=O)[C@H](C(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)N(C)C(=O)CN(C)C1=O PMATZTZNYRCHOR-CGLBZJNRSA-N 0.000 description 1
229930105110 Cyclosporin A Natural products 0.000 description 1
108010036949 Cyclosporine Proteins 0.000 description 1
108010036941 Cyclosporins Proteins 0.000 description 1
201000003883 Cystic fibrosis Diseases 0.000 description 1
108010000437 Deamino Arginine Vasopressin Proteins 0.000 description 1
108010051088 Delta Sleep-Inducing Peptide Proteins 0.000 description 1
102000016911 Deoxyribonucleases Human genes 0.000 description 1
108010053770 Deoxyribonucleases Proteins 0.000 description 1
108010002156 Depsipeptides Proteins 0.000 description 1
101800002242 Dermorphin Proteins 0.000 description 1
FHZPGIUBXYVUOY-VWGYHWLBSA-N Dermorphin Chemical compound C([C@H](N)C(=O)N[C@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CO)C(N)=O)C1=CC=C(O)C=C1 FHZPGIUBXYVUOY-VWGYHWLBSA-N 0.000 description 1
LTMHDMANZUZIPE-AMTYYWEZSA-N Digoxin Natural products O([C@H]1[C@H](C)O[C@H](O[C@@H]2C[C@@H]3[C@@](C)([C@@H]4[C@H]([C@]5(O)[C@](C)([C@H](O)C4)[C@H](C4=CC(=O)OC4)CC5)CC3)CC2)C[C@@H]1O)[C@H]1O[C@H](C)[C@@H](O[C@H]2O[C@@H](C)[C@H](O)[C@@H](O)C2)[C@@H](O)C1 LTMHDMANZUZIPE-AMTYYWEZSA-N 0.000 description 1
108010065372 Dynorphins Proteins 0.000 description 1
229930188669 Ebelactone Natural products 0.000 description 1
WOISDAHQBUYEAF-UHFFFAOYSA-N Ebelactone A Natural products CCC(C)C(O)C(C)C(=O)C(C)C=C(C)CC(C)C1OC(=O)C1C WOISDAHQBUYEAF-UHFFFAOYSA-N 0.000 description 1
IJWCGVPEDDQUDE-UHFFFAOYSA-N Elastatinal Natural products O=CC(C)NC(=O)C(CCC(N)=O)NC(=O)C(NC(=O)NC(CC(C)C)C(O)=O)C1CCN=C(N)N1 IJWCGVPEDDQUDE-UHFFFAOYSA-N 0.000 description 1
208000005189 Embolism Diseases 0.000 description 1
108010061435 Enalapril Proteins 0.000 description 1
201000009273 Endometriosis Diseases 0.000 description 1
102000005593 Endopeptidases Human genes 0.000 description 1
108010059378 Endopeptidases Proteins 0.000 description 1
241000792859 Enema Species 0.000 description 1
108010092674 Enkephalins Proteins 0.000 description 1
102000004190 Enzymes Human genes 0.000 description 1
108090000790 Enzymes Proteins 0.000 description 1
JKNGELGDDBUFHG-UHFFFAOYSA-N Esterastin Natural products CCCCCCC1C(CC(CC=CCC=CCCCCC)OC(=O)C(CC(N)=O)NC(C)=O)OC1=O JKNGELGDDBUFHG-UHFFFAOYSA-N 0.000 description 1
108010076282 Factor IX Proteins 0.000 description 1
108010023321 Factor VII Proteins 0.000 description 1
108010054265 Factor VIIa Proteins 0.000 description 1
108010080865 Factor XII Proteins 0.000 description 1
102000000429 Factor XII Human genes 0.000 description 1
108010090109 Fibrolase Proteins 0.000 description 1
102400000921 Gastrin Human genes 0.000 description 1
108010052343 Gastrins Proteins 0.000 description 1
208000015872 Gaucher disease Diseases 0.000 description 1
101000930822 Giardia intestinalis Dipeptidyl-peptidase 4 Proteins 0.000 description 1
102400000321 Glucagon Human genes 0.000 description 1
108060003199 Glucagon Proteins 0.000 description 1
102000004547 Glucosylceramidase Human genes 0.000 description 1
108010017544 Glucosylceramidase Proteins 0.000 description 1
102000005720 Glutathione transferase Human genes 0.000 description 1
108010070675 Glutathione transferase Proteins 0.000 description 1
102400000932 Gonadoliberin-1 Human genes 0.000 description 1
102000004269 Granulocyte Colony-Stimulating Factor Human genes 0.000 description 1
108010017080 Granulocyte Colony-Stimulating Factor Proteins 0.000 description 1
102000004457 Granulocyte-Macrophage Colony-Stimulating Factor Human genes 0.000 description 1
108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 description 1
206010019280 Heart failures Diseases 0.000 description 1
208000018565 Hemochromatosis Diseases 0.000 description 1
208000032843 Hemorrhage Diseases 0.000 description 1
241000700721 Hepatitis B virus Species 0.000 description 1
208000017604 Hodgkin disease Diseases 0.000 description 1
208000021519 Hodgkin lymphoma Diseases 0.000 description 1
208000010747 Hodgkins lymphoma Diseases 0.000 description 1
241000282412 Homo Species 0.000 description 1
101000777636 Homo sapiens ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 Proteins 0.000 description 1
101000911390 Homo sapiens Coagulation factor VIII Proteins 0.000 description 1
101500026183 Homo sapiens Gonadoliberin-1 Proteins 0.000 description 1
101000904173 Homo sapiens Progonadoliberin-1 Proteins 0.000 description 1
241000598436 Human T-cell lymphotropic virus Species 0.000 description 1
241000701044 Human gammaherpesvirus 4 Species 0.000 description 1
108010003272 Hyaluronate lyase Proteins 0.000 description 1
102000001974 Hyaluronidases Human genes 0.000 description 1
208000013038 Hypocalcemia Diseases 0.000 description 1
206010021333 Ileus paralytic Diseases 0.000 description 1
206010062016 Immunosuppression Diseases 0.000 description 1
206010061216 Infarction Diseases 0.000 description 1
102000014150 Interferons Human genes 0.000 description 1
108010050904 Interferons Proteins 0.000 description 1
108090000978 Interleukin-4 Proteins 0.000 description 1
108010002616 Interleukin-5 Proteins 0.000 description 1
108090001005 Interleukin-6 Proteins 0.000 description 1
108010002586 Interleukin-7 Proteins 0.000 description 1
108090001007 Interleukin-8 Proteins 0.000 description 1
108010063738 Interleukins Proteins 0.000 description 1
102000015696 Interleukins Human genes 0.000 description 1
201000005081 Intestinal Pseudo-Obstruction Diseases 0.000 description 1
208000004404 Intractable Pain Diseases 0.000 description 1
ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
108010000817 Leuprolide Proteins 0.000 description 1
108010006035 Metalloproteases Proteins 0.000 description 1
102000005741 Metalloproteases Human genes 0.000 description 1
102000014171 Milk Proteins Human genes 0.000 description 1
108010011756 Milk Proteins Proteins 0.000 description 1
101100286588 Mus musculus Igfl gene Proteins 0.000 description 1
241000186359 Mycobacterium Species 0.000 description 1
UBQYURCVBFRUQT-UHFFFAOYSA-N N-benzoyl-Ferrioxamine B Chemical compound CC(=O)N(O)CCCCCNC(=O)CCC(=O)N(O)CCCCCNC(=O)CCC(=O)N(O)CCCCCN UBQYURCVBFRUQT-UHFFFAOYSA-N 0.000 description 1
206010050502 Neuropathic ulcer Diseases 0.000 description 1
239000000020 Nitrocellulose Substances 0.000 description 1
108091028043 Nucleic acid sequence Proteins 0.000 description 1
108010016076 Octreotide Proteins 0.000 description 1
206010061137 Ocular toxicity Diseases 0.000 description 1
206010030113 Oedema Diseases 0.000 description 1
229930188236 Orienticin Natural products 0.000 description 1
241000283973 Oryctolagus cuniculus Species 0.000 description 1
208000010191 Osteitis Deformans Diseases 0.000 description 1
206010061535 Ovarian neoplasm Diseases 0.000 description 1
208000027868 Paget disease Diseases 0.000 description 1
206010033645 Pancreatitis Diseases 0.000 description 1
206010033649 Pancreatitis chronic Diseases 0.000 description 1
102000057297 Pepsin A Human genes 0.000 description 1
108090000284 Pepsin A Proteins 0.000 description 1
229930185974 Pepstanone Natural products 0.000 description 1
LTQCLFMNABRKSH-UHFFFAOYSA-N Phleomycin Natural products N=1C(C=2SC=C(N=2)C(N)=O)CSC=1CCNC(=O)C(C(O)C)NC(=O)C(C)C(O)C(C)NC(=O)C(C(OC1C(C(O)C(O)C(CO)O1)OC1C(C(OC(N)=O)C(O)C(CO)O1)O)C=1NC=NC=1)NC(=O)C1=NC(C(CC(N)=O)NCC(N)C(N)=O)=NC(N)=C1C LTQCLFMNABRKSH-UHFFFAOYSA-N 0.000 description 1
108010035235 Phleomycins Proteins 0.000 description 1
ZPHBZEQOLSRPAK-UHFFFAOYSA-N Phosphoramidon Natural products C=1NC2=CC=CC=C2C=1CC(C(O)=O)NC(=O)C(CC(C)C)NP(O)(=O)OC1OC(C)C(O)C(O)C1O ZPHBZEQOLSRPAK-UHFFFAOYSA-N 0.000 description 1
241000224016 Plasmodium Species 0.000 description 1
239000004793 Polystyrene Substances 0.000 description 1
241000243142 Porifera Species 0.000 description 1
LRXVQHCIMZSTJH-UHFFFAOYSA-N Poststatin Natural products CC(C)C(N)C(=O)NC(C(C)C)C(=O)NC(CC)C(=O)C(=O)NC(CC(C)C)C(=O)NC(C(C)C)C(O)=O LRXVQHCIMZSTJH-UHFFFAOYSA-N 0.000 description 1
208000006664 Precursor Cell Lymphoblastic Leukemia-Lymphoma Diseases 0.000 description 1
208000004210 Pressure Ulcer Diseases 0.000 description 1
102100024028 Progonadoliberin-1 Human genes 0.000 description 1
102000003946 Prolactin Human genes 0.000 description 1
108010057464 Prolactin Proteins 0.000 description 1
102000007327 Protamines Human genes 0.000 description 1
108010007568 Protamines Proteins 0.000 description 1
101800004937 Protein C Proteins 0.000 description 1
241000589516 Pseudomonas Species 0.000 description 1
108020004511 Recombinant DNA Proteins 0.000 description 1
102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
102000003743 Relaxin Human genes 0.000 description 1
108090000103 Relaxin Proteins 0.000 description 1
208000006265 Renal cell carcinoma Diseases 0.000 description 1
102400000827 Saposin-D Human genes 0.000 description 1
101800001700 Saposin-D Proteins 0.000 description 1
241000242678 Schistosoma Species 0.000 description 1
206010039710 Scleroderma Diseases 0.000 description 1
108010086019 Secretin Proteins 0.000 description 1
102100037505 Secretin Human genes 0.000 description 1
MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
241000700584 Simplexvirus Species 0.000 description 1
DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 1
102100022831 Somatoliberin Human genes 0.000 description 1
101710142969 Somatoliberin Proteins 0.000 description 1
102000005157 Somatostatin Human genes 0.000 description 1
108010056088 Somatostatin Proteins 0.000 description 1
241000191940 Staphylococcus Species 0.000 description 1
208000007107 Stomach Ulcer Diseases 0.000 description 1
241000194017 Streptococcus Species 0.000 description 1
QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
OUUQCZGPVNCOIJ-UHFFFAOYSA-M Superoxide Chemical compound [O-][O] OUUQCZGPVNCOIJ-UHFFFAOYSA-M 0.000 description 1
101000996723 Sus scrofa Gonadotropin-releasing hormone receptor Proteins 0.000 description 1
101150109894 TGFA gene Proteins 0.000 description 1
108700012920 TNF Proteins 0.000 description 1
206010043118 Tardive Dyskinesia Diseases 0.000 description 1
208000001435 Thromboembolism Diseases 0.000 description 1
108010046075 Thymosin Proteins 0.000 description 1
102000007501 Thymosin Human genes 0.000 description 1
102000011923 Thyrotropin Human genes 0.000 description 1
108010061174 Thyrotropin Proteins 0.000 description 1
206010044245 Toxic optic neuropathy Diseases 0.000 description 1
206010052779 Transplant rejections Diseases 0.000 description 1
241000223104 Trypanosoma Species 0.000 description 1
108090000631 Trypsin Proteins 0.000 description 1
102000004142 Trypsin Human genes 0.000 description 1
102100032807 Tumor necrosis factor-inducible gene 6 protein Human genes 0.000 description 1
101710169430 Tumor necrosis factor-inducible gene 6 protein Proteins 0.000 description 1
102000018594 Tumour necrosis factor Human genes 0.000 description 1
108050007852 Tumour necrosis factor Proteins 0.000 description 1
108010076164 Tyrocidine Proteins 0.000 description 1
208000025865 Ulcer Diseases 0.000 description 1
GXBMIBRIOWHPDT-UHFFFAOYSA-N Vasopressin Natural products N1C(=O)C(CC=2C=C(O)C=CC=2)NC(=O)C(N)CSSCC(C(=O)N2C(CCC2)C(=O)NC(CCCN=C(N)N)C(=O)NCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(CCC(N)=O)NC(=O)C1CC1=CC=CC=C1 GXBMIBRIOWHPDT-UHFFFAOYSA-N 0.000 description 1
108010004977 Vasopressins Proteins 0.000 description 1
102000002852 Vasopressins Human genes 0.000 description 1
101710200894 Versican core protein Proteins 0.000 description 1
102100028437 Versican core protein Human genes 0.000 description 1
241000700605 Viruses Species 0.000 description 1
206010052428 Wound Diseases 0.000 description 1
JKNGELGDDBUFHG-JJPNXARGSA-N [(2S,4Z,7Z)-1-[(2S,3S)-3-hexyl-4-oxooxetan-2-yl]trideca-4,7-dien-2-yl] (2S)-2-acetamido-4-amino-4-oxobutanoate Chemical compound CCCCCC[C@H]1[C@H](C[C@H](C\C=C/C\C=C/CCCCC)OC(=O)[C@H](CC(N)=O)NC(C)=O)OC1=O JKNGELGDDBUFHG-JJPNXARGSA-N 0.000 description 1
230000005856 abnormality Effects 0.000 description 1
206010000269 abscess Diseases 0.000 description 1
238000009825 accumulation Methods 0.000 description 1
239000002253 acid Substances 0.000 description 1
239000000061 acid fraction Substances 0.000 description 1
108010020588 actaplanin Proteins 0.000 description 1
BDNDRNLSLGGULA-UHFFFAOYSA-N actaplanin Chemical compound C=1C2=CC=C(O)C=1C1=C(OC3C(C(O)C(O)C(CO)O3)O)C=C(O)C=C1C(C(=O)OC)NC(=O)C1NC(=O)C2NC(=O)C2NC(=O)C(C=3C=C(C(=C(O)C=3)C)OC=3C(O)=CC=C(C=3)C(N)C(=O)N3)NC(=O)C3CC(C=C3)=CC=C3OC(C=3OC4C(C(O)C(O)C(CO)O4)O)=CC2=CC=3OC(C(=C2)Cl)=CC=C2C1OC1CC(N)C(O)C(C)O1 BDNDRNLSLGGULA-UHFFFAOYSA-N 0.000 description 1
229950002379 actaplanin Drugs 0.000 description 1
229930183665 actinomycin Natural products 0.000 description 1
XJLATMLVMSFZBN-VYDXJSESSA-N actinonin Chemical compound CCCCC[C@H](CC(=O)NO)C(=O)N[C@@H](C(C)C)C(=O)N1CCC[C@H]1CO XJLATMLVMSFZBN-VYDXJSESSA-N 0.000 description 1
XJLATMLVMSFZBN-UHFFFAOYSA-N actinonine Natural products CCCCCC(CC(=O)NO)C(=O)NC(C(C)C)C(=O)N1CCCC1CO XJLATMLVMSFZBN-UHFFFAOYSA-N 0.000 description 1
239000012190 activator Substances 0.000 description 1
230000001464 adherent effect Effects 0.000 description 1
230000001919 adrenal effect Effects 0.000 description 1
230000002411 adverse Effects 0.000 description 1
238000001042 affinity chromatography Methods 0.000 description 1
239000011543 agarose gel Substances 0.000 description 1
108700029371 albomycin Proteins 0.000 description 1
229910052782 aluminium Inorganic materials 0.000 description 1
XAGFODPZIPBFFR-UHFFFAOYSA-N aluminium Chemical compound [Al] XAGFODPZIPBFFR-UHFFFAOYSA-N 0.000 description 1
108010052590 amastatin Proteins 0.000 description 1
QFAADIRHLBXJJS-ZAZJUGBXSA-N amastatin Chemical compound CC(C)C[C@@H](N)[C@H](O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@H](C(O)=O)CC(O)=O QFAADIRHLBXJJS-ZAZJUGBXSA-N 0.000 description 1
231100000540 amenorrhea Toxicity 0.000 description 1
125000003277 amino group Chemical group 0.000 description 1
239000000908 ammonium hydroxide Substances 0.000 description 1
238000004458 analytical method Methods 0.000 description 1
108010072788 angiogenin Proteins 0.000 description 1
229940044094 angiotensin-converting-enzyme inhibitor Drugs 0.000 description 1
125000000129 anionic group Chemical group 0.000 description 1
208000025009 anogenital human papillomavirus infection Diseases 0.000 description 1
201000004201 anogenital venereal wart Diseases 0.000 description 1
229940019748 antifibrinolytic proteinase inhibitors Drugs 0.000 description 1
239000002246 antineoplastic agent Substances 0.000 description 1
229960005348 antithrombin iii Drugs 0.000 description 1
230000036528 appetite Effects 0.000 description 1
235000019789 appetite Nutrition 0.000 description 1
229960004405 aprotinin Drugs 0.000 description 1
239000007864 aqueous solution Substances 0.000 description 1
QSDFMNDRKUYSFI-MEQJCLHWSA-N ardacin Chemical compound N1C(=O)C(NC)C(C=2)=CC=C(O)C=2OC(C=2)=CC(O)=C(Cl)C=2C(C(NC2C(=O)NC3C(=O)NC(C(NC(C4=CC(O)=CC(O)=C4C=4C(O)=CC=C3C=4)C(O)=O)=O)C(O)C3=CC(Cl)=C(C(=C3)Cl)O3)=O)NC(=O)C1C(O)C(C=C1Cl)=CC=C1OC1=CC2=CC3=C1OC1O[C@H](C(O)=O)[C@@H](O)[C@H](O)[C@H]1NC=O QSDFMNDRKUYSFI-MEQJCLHWSA-N 0.000 description 1
229950001376 ardacin Drugs 0.000 description 1
ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
KBZOIRJILGZLEJ-LGYYRGKSSA-N argipressin Chemical compound C([C@H]1C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CSSC[C@@H](C(N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N1)=O)N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCN=C(N)N)C(=O)NCC(N)=O)C1=CC=CC=C1 KBZOIRJILGZLEJ-LGYYRGKSSA-N 0.000 description 1
230000004872 arterial blood pressure Effects 0.000 description 1
229960003272 asparaginase Drugs 0.000 description 1
DCXYFEDJOCDNAF-UHFFFAOYSA-M asparaginate Chemical compound [O-]C(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-M 0.000 description 1
239000003696 aspartic proteinase inhibitor Substances 0.000 description 1
FIVPIPIDMRVLAY-UHFFFAOYSA-N aspergillin Natural products C1C2=CC=CC(O)C2N2C1(SS1)C(=O)N(C)C1(CO)C2=O FIVPIPIDMRVLAY-UHFFFAOYSA-N 0.000 description 1
239000012298 atmosphere Substances 0.000 description 1
230000001746 atrial effect Effects 0.000 description 1
230000001363 autoimmune Effects 0.000 description 1
108010053278 avoparcin Proteins 0.000 description 1
JWFVWARSGMYXRN-HTQQBIQNSA-N avoparcin Chemical compound O([C@H]1[C@H](C(N[C@H](C(=O)N[C@H]2C(=O)N[C@H]3C(=O)N[C@H](C(N[C@H](C4=CC(O)=CC(O)=C4C=4C(O)=CC=C3C=4)C(O)=O)=O)CC3=C(O[C@@H]4O[C@@H](C)[C@H](O)[C@H](N)C4)C=C(C(=C3)Cl)OC=3C=C2C=C(C=3O[C@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O2)O[C@@H]2O[C@@H](C)[C@H](O)[C@H](N)C2)OC2=CC=C1C=C2)C=1C=CC(O)=CC=1)=O)NC(=O)[C@@H](NC)C=1C=CC(O[C@H]2[C@@H]([C@H](O)[C@@H](O)[C@H](C)O2)O)=CC=1)[C@@H]1O[C@@H](CO)[C@H](O)[C@@H](O)[C@H]1O JWFVWARSGMYXRN-HTQQBIQNSA-N 0.000 description 1
229950001335 avoparcin Drugs 0.000 description 1
235000019377 avoparcin Nutrition 0.000 description 1
229960003071 bacitracin Drugs 0.000 description 1
229930184125 bacitracin Natural products 0.000 description 1
CLKOFPXJLQSYAH-ABRJDSQDSA-N bacitracin A Chemical compound C1SC([C@@H](N)[C@@H](C)CC)=N[C@@H]1C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]1C(=O)N[C@H](CCCN)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2N=CNC=2)C(=O)N[C@H](CC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)NCCCC1 CLKOFPXJLQSYAH-ABRJDSQDSA-N 0.000 description 1
108010079684 beauvericin Proteins 0.000 description 1
GYSCAQFHASJXRS-FFCOJMSVSA-N beauvericin Chemical compound C([C@H]1C(=O)O[C@@H](C(N(C)[C@@H](CC=2C=CC=CC=2)C(=O)O[C@@H](C(=O)N(C)[C@@H](CC=2C=CC=CC=2)C(=O)O[C@@H](C(=O)N1C)C(C)C)C(C)C)=O)C(C)C)C1=CC=CC=C1 GYSCAQFHASJXRS-FFCOJMSVSA-N 0.000 description 1
GYSCAQFHASJXRS-UHFFFAOYSA-N beauvericin Natural products CN1C(=O)C(C(C)C)OC(=O)C(CC=2C=CC=CC=2)N(C)C(=O)C(C(C)C)OC(=O)C(CC=2C=CC=CC=2)N(C)C(=O)C(C(C)C)OC(=O)C1CC1=CC=CC=C1 GYSCAQFHASJXRS-UHFFFAOYSA-N 0.000 description 1
230000009286 beneficial effect Effects 0.000 description 1
229960001561 bleomycin Drugs 0.000 description 1
OYVAGSVQBOHSSS-UAPAGMARSA-O bleomycin A2 Chemical compound N([C@H](C(=O)N[C@H](C)[C@@H](O)[C@H](C)C(=O)N[C@@H]([C@H](O)C)C(=O)NCCC=1SC=C(N=1)C=1SC=C(N=1)C(=O)NCCC[S+](C)C)[C@@H](O[C@H]1[C@H]([C@@H](O)[C@H](O)[C@H](CO)O1)O[C@@H]1[C@H]([C@@H](OC(N)=O)[C@H](O)[C@@H](CO)O1)O)C=1N=CNC=1)C(=O)C1=NC([C@H](CC(N)=O)NC[C@H](N)C(N)=O)=NC(N)=C1C OYVAGSVQBOHSSS-UAPAGMARSA-O 0.000 description 1
210000004369 blood Anatomy 0.000 description 1
239000008280 blood Substances 0.000 description 1
230000023555 blood coagulation Effects 0.000 description 1
210000004204 blood vessel Anatomy 0.000 description 1
239000005388 borosilicate glass Substances 0.000 description 1
210000000481 breast Anatomy 0.000 description 1
125000000484 butyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
229960000830 captopril Drugs 0.000 description 1
FAKRSMQSSFJEIM-RQJHMYQMSA-N captopril Chemical compound SC[C@@H](C)C(=O)N1CCC[C@H]1C(O)=O FAKRSMQSSFJEIM-RQJHMYQMSA-N 0.000 description 1
YZBQHRLRFGPBSL-RXMQYKEDSA-N carbapenem Chemical compound C1C=CN2C(=O)C[C@H]21 YZBQHRLRFGPBSL-RXMQYKEDSA-N 0.000 description 1
150000001718 carbodiimides Chemical class 0.000 description 1
210000000845 cartilage Anatomy 0.000 description 1
239000005018 casein Substances 0.000 description 1
BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
235000021240 caseins Nutrition 0.000 description 1
125000002091 cationic group Chemical group 0.000 description 1
230000021164 cell adhesion Effects 0.000 description 1
230000012292 cell migration Effects 0.000 description 1
230000004663 cell proliferation Effects 0.000 description 1
238000012512 characterization method Methods 0.000 description 1
238000002655 chelation therapy Methods 0.000 description 1
AOXOCDRNSPFDPE-UKEONUMOSA-N chembl413654 Chemical compound C([C@H](C(=O)NCC(=O)N[C@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@H](CCSC)C(=O)N[C@H](CC(O)=O)C(=O)N[C@H](CC=1C=CC=CC=1)C(N)=O)NC(=O)[C@@H](C)NC(=O)[C@@H](CCC(O)=O)NC(=O)[C@@H](CCC(O)=O)NC(=O)[C@@H](CCC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H]1N(CCC1)C(=O)CNC(=O)[C@@H](N)CCC(O)=O)C1=CC=C(O)C=C1 AOXOCDRNSPFDPE-UKEONUMOSA-N 0.000 description 1
230000035606 childbirth Effects 0.000 description 1
ZPEIMTDSQAKGNT-UHFFFAOYSA-N chlorpromazine Chemical compound C1=C(Cl)C=C2N(CCCN(C)C)C3=CC=CC=C3SC2=C1 ZPEIMTDSQAKGNT-UHFFFAOYSA-N 0.000 description 1
229960001076 chlorpromazine Drugs 0.000 description 1
229940107137 cholecystokinin Drugs 0.000 description 1
230000001684 chronic effect Effects 0.000 description 1
208000020832 chronic kidney disease Diseases 0.000 description 1
108010086192 chymostatin Proteins 0.000 description 1
229960001265 ciclosporin Drugs 0.000 description 1
229930193282 clathrin Natural products 0.000 description 1
238000010367 cloning Methods 0.000 description 1
230000015271 coagulation Effects 0.000 description 1
238000005345 coagulation Methods 0.000 description 1
229920001436 collagen Polymers 0.000 description 1
229920001577 copolymer Chemical class 0.000 description 1
ZOEFCCMDUURGSE-SQKVDDBVSA-N cosyntropin Chemical compound C([C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(O)=O)NC(=O)[C@@H](N)CO)C1=CC=C(O)C=C1 ZOEFCCMDUURGSE-SQKVDDBVSA-N 0.000 description 1
239000002852 cysteine proteinase inhibitor Substances 0.000 description 1
229940127089 cytotoxic agent Drugs 0.000 description 1
238000001804 debridement Methods 0.000 description 1
230000002950 deficient Effects 0.000 description 1
230000000881 depressing effect Effects 0.000 description 1
238000001212 derivatisation Methods 0.000 description 1
229960004281 desmopressin Drugs 0.000 description 1
NFLWUMRGJYTJIN-NXBWRCJVSA-N desmopressin Chemical compound C([C@H]1C(=O)N[C@H](C(N[C@@H](CC(N)=O)C(=O)N[C@@H](CSSCCC(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(N)=O)=O)CCC(=O)N)C1=CC=CC=C1 NFLWUMRGJYTJIN-NXBWRCJVSA-N 0.000 description 1
238000001514 detection method Methods 0.000 description 1
238000000502 dialysis Methods 0.000 description 1
230000001079 digestive effect Effects 0.000 description 1
LTMHDMANZUZIPE-PUGKRICDSA-N digoxin Chemical compound C1[C@H](O)[C@H](O)[C@@H](C)O[C@H]1O[C@@H]1[C@@H](C)O[C@@H](O[C@@H]2[C@H](O[C@@H](O[C@@H]3C[C@@H]4[C@]([C@@H]5[C@H]([C@]6(CC[C@@H]([C@@]6(C)[C@H](O)C5)C=5COC(=O)C=5)O)CC4)(C)CC3)C[C@@H]2O)C)C[C@@H]1O LTMHDMANZUZIPE-PUGKRICDSA-N 0.000 description 1
229960005156 digoxin Drugs 0.000 description 1
LTMHDMANZUZIPE-UHFFFAOYSA-N digoxine Natural products C1C(O)C(O)C(C)OC1OC1C(C)OC(OC2C(OC(OC3CC4C(C5C(C6(CCC(C6(C)C(O)C5)C=5COC(=O)C=5)O)CC4)(C)CC3)CC2O)C)CC1O LTMHDMANZUZIPE-UHFFFAOYSA-N 0.000 description 1
238000010790 dilution Methods 0.000 description 1
239000012895 dilution Substances 0.000 description 1
229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 1
150000002016 disaccharides Chemical class 0.000 description 1
230000009429 distress Effects 0.000 description 1
239000002934 diuretic Substances 0.000 description 1
230000004064 dysfunction Effects 0.000 description 1
201000006549 dyspepsia Diseases 0.000 description 1
230000002526 effect on cardiovascular system Effects 0.000 description 1
230000002500 effect on skin Effects 0.000 description 1
108010039262 elastatinal Proteins 0.000 description 1
239000003792 electrolyte Substances 0.000 description 1
229960000873 enalapril Drugs 0.000 description 1
GBXSMTUPTTWBMN-XIRDDKMYSA-N enalapril Chemical compound C([C@@H](C(=O)OCC)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(O)=O)CC1=CC=CC=C1 GBXSMTUPTTWBMN-XIRDDKMYSA-N 0.000 description 1
230000002124 endocrine Effects 0.000 description 1
229940066758 endopeptidases Drugs 0.000 description 1
239000007920 enema Substances 0.000 description 1
229940095399 enema Drugs 0.000 description 1
238000005516 engineering process Methods 0.000 description 1
229930191716 enniatin Natural products 0.000 description 1
MIZMDSVSLSIMSC-VYLWARHZSA-N enniatin B Chemical compound CC(C)[C@H]1OC(=O)[C@H](C(C)C)N(C)C(=O)[C@@H](C(C)C)OC(=O)[C@H](C(C)C)N(C)C(=O)[C@@H](C(C)C)OC(=O)[C@H](C(C)C)N(C)C1=O MIZMDSVSLSIMSC-VYLWARHZSA-N 0.000 description 1
108010081513 enniatins Proteins 0.000 description 1
108010013356 eremomycin Proteins 0.000 description 1
UECIPBUIMXSXEI-BNSVOVDNSA-N eremomycin Chemical compound O([C@@H]1C2=CC=C(C=C2)OC=2C=C3C=C(C=2O[C@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O2)O[C@@H]2O[C@@H](C)[C@H](O)[C@@](C)(N)C2)OC2=CC=C(C=C2Cl)[C@@H](O)[C@H](C(N[C@@H](CC(N)=O)C(=O)N[C@H]3C(=O)N[C@H]2C(=O)N[C@@H]1C(N[C@@H](C1=CC(O)=CC(O)=C1C=1C(O)=CC=C2C=1)C(O)=O)=O)=O)NC(=O)[C@@H](CC(C)C)NC)[C@H]1C[C@](C)(N)[C@@H](O)[C@H](C)O1 UECIPBUIMXSXEI-BNSVOVDNSA-N 0.000 description 1
UECIPBUIMXSXEI-UHFFFAOYSA-N eremomycin Natural products C=1C2=CC=C(O)C=1C1=C(O)C=C(O)C=C1C(C(O)=O)NC(=O)C1NC(=O)C2NC(=O)C2NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(CC(C)C)NC)C(O)C(C=C3Cl)=CC=C3OC(C=3OC4C(C(O)C(O)C(CO)O4)OC4OC(C)C(O)C(C)(N)C4)=CC2=CC=3OC(C=C2)=CC=C2C1OC1CC(C)(N)C(O)C(C)O1 UECIPBUIMXSXEI-UHFFFAOYSA-N 0.000 description 1
229940105423 erythropoietin Drugs 0.000 description 1
229960004222 factor ix Drugs 0.000 description 1
229940012413 factor vii Drugs 0.000 description 1
229940012414 factor viia Drugs 0.000 description 1
239000003527 fibrinolytic agent Substances 0.000 description 1
230000003480 fibrinolytic effect Effects 0.000 description 1
239000005308 flint glass Substances 0.000 description 1
239000012530 fluid Substances 0.000 description 1
235000019253 formic acid Nutrition 0.000 description 1
238000009472 formulation Methods 0.000 description 1
108010090705 foroxymithine Proteins 0.000 description 1
210000004051 gastric juice Anatomy 0.000 description 1
230000009395 genetic defect Effects 0.000 description 1
230000002068 genetic effect Effects 0.000 description 1
FIVPIPIDMRVLAY-RBJBARPLSA-N gliotoxin Chemical compound C1C2=CC=C[C@H](O)[C@H]2N2[C@]1(SS1)C(=O)N(C)[C@@]1(CO)C2=O FIVPIPIDMRVLAY-RBJBARPLSA-N 0.000 description 1
229940103893 gliotoxin Drugs 0.000 description 1
229930190252 gliotoxin Natural products 0.000 description 1
MASNOZXLGMXCHN-ZLPAWPGGSA-N glucagon Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 MASNOZXLGMXCHN-ZLPAWPGGSA-N 0.000 description 1
229960004666 glucagon Drugs 0.000 description 1
230000013595 glycosylation Effects 0.000 description 1
238000006206 glycosylation reaction Methods 0.000 description 1
230000002710 gonadal effect Effects 0.000 description 1
XLXSAKCOAKORKW-AQJXLSMYSA-N gonadorelin Chemical compound C([C@@H](C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N1[C@@H](CCC1)C(=O)NCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@H]1NC(=O)CC1)C1=CC=C(O)C=C1 XLXSAKCOAKORKW-AQJXLSMYSA-N 0.000 description 1
XLXSAKCOAKORKW-UHFFFAOYSA-N gonadorelin Chemical compound C1CCC(C(=O)NCC(N)=O)N1C(=O)C(CCCN=C(N)N)NC(=O)C(CC(C)C)NC(=O)CNC(=O)C(NC(=O)C(CO)NC(=O)C(CC=1C2=CC=CC=C2NC=1)NC(=O)C(CC=1NC=NC=1)NC(=O)C1NC(=O)CC1)CC1=CC=C(O)C=C1 XLXSAKCOAKORKW-UHFFFAOYSA-N 0.000 description 1
229960001442 gonadorelin Drugs 0.000 description 1
IUAYMJGZBVDSGL-XNNAEKOYSA-N gramicidin S Chemical compound C([C@@H]1C(=O)N2CCC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CCCN)C(=O)N[C@H](C(N[C@H](CC=2C=CC=CC=2)C(=O)N2CCC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CCCN)C(=O)N[C@@H](CC(C)C)C(=O)N1)C(C)C)=O)CC(C)C)C(C)C)C1=CC=CC=C1 IUAYMJGZBVDSGL-XNNAEKOYSA-N 0.000 description 1
229950009774 gramicidin s Drugs 0.000 description 1
210000003714 granulocyte Anatomy 0.000 description 1
108010077687 gratisin Proteins 0.000 description 1
KIUGLYLJMHCDMF-AHAYUKIASA-N gratisin Chemical compound C([C@@H]1C(=O)N[C@H](C(=O)N[C@@H](CCCN)C(=O)N[C@H](C(N[C@H](CC=2C=CC=CC=2)C(=O)N2CCC[C@H]2C(=O)N[C@H](CC=2C=CC(O)=CC=2)C(=O)N[C@H](C(=O)N[C@@H](CCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](CC=2C=CC=CC=2)C(=O)N2CCC[C@H]2C(=O)N1)C(C)C)=O)CC(C)C)C(C)C)C1=CC=C(O)C=C1 KIUGLYLJMHCDMF-AHAYUKIASA-N 0.000 description 1
239000000122 growth hormone Substances 0.000 description 1
201000009277 hairy cell leukemia Diseases 0.000 description 1
125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 1
229960002773 hyaluronidase Drugs 0.000 description 1
230000007062 hydrolysis Effects 0.000 description 1
238000006460 hydrolysis reaction Methods 0.000 description 1
108010058710 hydroxypepstatin Proteins 0.000 description 1
230000000705 hypocalcaemia Effects 0.000 description 1
238000002649 immunization Methods 0.000 description 1
230000003053 immunization Effects 0.000 description 1
230000001506 immunosuppresive effect Effects 0.000 description 1
230000002637 immunotoxin Effects 0.000 description 1
229940051026 immunotoxin Drugs 0.000 description 1
239000002596 immunotoxin Substances 0.000 description 1
231100000608 immunotoxin Toxicity 0.000 description 1
230000006872 improvement Effects 0.000 description 1
230000007574 infarction Effects 0.000 description 1
208000015181 infectious disease Diseases 0.000 description 1
231100000535 infertility Toxicity 0.000 description 1
230000002401 inhibitory effect Effects 0.000 description 1
ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 1
238000003780 insertion Methods 0.000 description 1
230000037431 insertion Effects 0.000 description 1
230000002608 insulinlike Effects 0.000 description 1
230000003993 interaction Effects 0.000 description 1
229940047122 interleukins Drugs 0.000 description 1
238000007913 intrathecal administration Methods 0.000 description 1
210000003734 kidney Anatomy 0.000 description 1
230000006651 lactation Effects 0.000 description 1
GFIJNRVAKGFPGQ-LIJARHBVSA-N leuprolide Chemical compound CCNC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@H]1NC(=O)CC1)CC1=CC=C(O)C=C1 GFIJNRVAKGFPGQ-LIJARHBVSA-N 0.000 description 1
229960004338 leuprorelin Drugs 0.000 description 1
230000000670 limiting effect Effects 0.000 description 1
125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
229920002521 macromolecule Polymers 0.000 description 1
210000002540 macrophage Anatomy 0.000 description 1
208000027202 mammary Paget disease Diseases 0.000 description 1
230000001404 mediated effect Effects 0.000 description 1
239000012528 membrane Substances 0.000 description 1
229910052751 metal Inorganic materials 0.000 description 1
239000002184 metal Substances 0.000 description 1
230000002906 microbiologic effect Effects 0.000 description 1
230000005012 migration Effects 0.000 description 1
238000013508 migration Methods 0.000 description 1
235000021239 milk protein Nutrition 0.000 description 1
230000004048 modification Effects 0.000 description 1
238000012986 modification Methods 0.000 description 1
230000004899 motility Effects 0.000 description 1
210000002200 mouth mucosa Anatomy 0.000 description 1
201000006417 multiple sclerosis Diseases 0.000 description 1
229960003816 muromonab-cd3 Drugs 0.000 description 1
230000002107 myocardial effect Effects 0.000 description 1
208000010125 myocardial infarction Diseases 0.000 description 1
230000003533 narcotic effect Effects 0.000 description 1
230000001452 natriuretic effect Effects 0.000 description 1
210000005036 nerve Anatomy 0.000 description 1
230000000926 neurological effect Effects 0.000 description 1
201000001119 neuropathy Diseases 0.000 description 1
230000007823 neuropathy Effects 0.000 description 1
208000004235 neutropenia Diseases 0.000 description 1
229920001220 nitrocellulos Polymers 0.000 description 1
229910052757 nitrogen Inorganic materials 0.000 description 1
239000000041 non-steroidal anti-inflammatory agent Substances 0.000 description 1
229940021182 non-steroidal anti-inflammatory drug Drugs 0.000 description 1
231100000956 nontoxicity Toxicity 0.000 description 1
229960002700 octreotide Drugs 0.000 description 1
231100000327 ocular toxicity Toxicity 0.000 description 1
238000011275 oncology therapy Methods 0.000 description 1
229940005483 opioid analgesics Drugs 0.000 description 1
230000036407 pain Effects 0.000 description 1
201000007620 paralytic ileus Diseases 0.000 description 1
230000000849 parathyroid Effects 0.000 description 1
239000002245 particle Substances 0.000 description 1
230000037361 pathway Effects 0.000 description 1
229950011098 pendetide Drugs 0.000 description 1
230000035515 penetration Effects 0.000 description 1
229940111202 pepsin Drugs 0.000 description 1
108010091212 pepstatin Proteins 0.000 description 1
229950000964 pepstatin Drugs 0.000 description 1
FAXGPCHRFPCXOO-LXTPJMTPSA-N pepstatin A Chemical compound OC(=O)C[C@H](O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)C[C@H](O)[C@H](CC(C)C)NC(=O)[C@H](C(C)C)NC(=O)[C@H](C(C)C)NC(=O)CC(C)C FAXGPCHRFPCXOO-LXTPJMTPSA-N 0.000 description 1
238000010647 peptide synthesis reaction Methods 0.000 description 1
108010072906 phosphoramidon Proteins 0.000 description 1
BWSDNRQVTFZQQD-AYVHNPTNSA-N phosphoramidon Chemical compound O([P@@](O)(=O)N[C@H](CC(C)C)C(=O)N[C@H](CC=1[C]2C=CC=CC2=NC=1)C(O)=O)[C@H]1O[C@@H](C)[C@H](O)[C@@H](O)[C@@H]1O BWSDNRQVTFZQQD-AYVHNPTNSA-N 0.000 description 1
230000036470 plasma concentration Effects 0.000 description 1
239000013612 plasmid Substances 0.000 description 1
229940012957 plasmin Drugs 0.000 description 1
239000004033 plastic Substances 0.000 description 1
229920003023 plastic Polymers 0.000 description 1
210000004910 pleural fluid Anatomy 0.000 description 1
238000003752 polymerase chain reaction Methods 0.000 description 1
229920001184 polypeptide Polymers 0.000 description 1
239000003910 polypeptide antibiotic agent Substances 0.000 description 1
229920002223 polystyrene Polymers 0.000 description 1
108010080180 poststatin Proteins 0.000 description 1
OXCMYAYHXIHQOA-UHFFFAOYSA-N potassium;[2-butyl-5-chloro-3-[[4-[2-(1,2,4-triaza-3-azanidacyclopenta-1,4-dien-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol Chemical compound [K+].CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C2=N[N-]N=N2)C=C1 OXCMYAYHXIHQOA-UHFFFAOYSA-N 0.000 description 1
239000002244 precipitate Substances 0.000 description 1
108010020676 probestin Proteins 0.000 description 1
229940097325 prolactin Drugs 0.000 description 1
230000035755 proliferation Effects 0.000 description 1
229940048914 protamine Drugs 0.000 description 1
229960000856 protein c Drugs 0.000 description 1
230000005855 radiation Effects 0.000 description 1
229940051022 radioimmunoconjugate Drugs 0.000 description 1
238000001959 radiotherapy Methods 0.000 description 1
230000029865 regulation of blood pressure Effects 0.000 description 1
230000008439 repair process Effects 0.000 description 1
230000004044 response Effects 0.000 description 1
206010039073 rheumatoid arthritis Diseases 0.000 description 1
238000009781 safety test method Methods 0.000 description 1
229960002101 secretin Drugs 0.000 description 1
OWMZNFCDEHGFEP-NFBCVYDUSA-N secretin human Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(N)=O)[C@@H](C)O)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)C1=CC=CC=C1 OWMZNFCDEHGFEP-NFBCVYDUSA-N 0.000 description 1
230000028327 secretion Effects 0.000 description 1
230000035945 sensitivity Effects 0.000 description 1
239000003001 serine protease inhibitor Substances 0.000 description 1
210000002966 serum Anatomy 0.000 description 1
108010046596 sideromycins Proteins 0.000 description 1
IZTQOLKUZKXIRV-YRVFCXMDSA-N sincalide Chemical compound C([C@@H](C(=O)N[C@@H](CCSC)C(=O)NCC(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC=CC=1)C(N)=O)NC(=O)[C@@H](N)CC(O)=O)C1=CC=C(OS(O)(=O)=O)C=C1 IZTQOLKUZKXIRV-YRVFCXMDSA-N 0.000 description 1
238000002741 site-directed mutagenesis Methods 0.000 description 1
238000004513 sizing Methods 0.000 description 1
230000009645 skeletal growth Effects 0.000 description 1
229940083575 sodium dodecyl sulfate Drugs 0.000 description 1
229940049529 sodium hyaluronate 20 mg/ml Drugs 0.000 description 1
235000019333 sodium laurylsulphate Nutrition 0.000 description 1
NHXLMOGPVYXJNR-ATOGVRKGSA-N somatostatin Chemical compound C([C@H]1C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CSSC[C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC=2C3=CC=CC=C3NC=2)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N1)[C@@H](C)O)NC(=O)CNC(=O)[C@H](C)N)C(O)=O)=O)[C@H](O)C)C1=CC=CC=C1 NHXLMOGPVYXJNR-ATOGVRKGSA-N 0.000 description 1
229960000553 somatostatin Drugs 0.000 description 1
238000000527 sonication Methods 0.000 description 1
241000894007 species Species 0.000 description 1
230000002269 spontaneous effect Effects 0.000 description 1
206010041823 squamous cell carcinoma Diseases 0.000 description 1
238000010561 standard procedure Methods 0.000 description 1
XTWDJNIPHUFHNS-GXHLCREISA-N stenothricin Chemical compound OS(=O)(=O)CC(NC)C(=O)NC1C(C)OC(=O)CN(C)C(=O)C(CCCCN)NC(=O)C(CO)NC(=O)C(C(C)C)NC(=O)\C(=C\C)NC(=O)C(CN)NC(=O)C(CO)NC1=O XTWDJNIPHUFHNS-GXHLCREISA-N 0.000 description 1
239000008174 sterile solution Substances 0.000 description 1
239000000758 substrate Substances 0.000 description 1
235000000346 sugar Nutrition 0.000 description 1
150000008163 sugars Chemical class 0.000 description 1
QAOWNCQODCNURD-UHFFFAOYSA-N sulfuric acid Substances OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 1
238000001356 surgical procedure Methods 0.000 description 1
208000011580 syndromic disease Diseases 0.000 description 1
238000003786 synthesis reaction Methods 0.000 description 1
210000001550 testis Anatomy 0.000 description 1
229960001423 tetracosactide Drugs 0.000 description 1
238000002560 therapeutic procedure Methods 0.000 description 1
LCJVIYPJPCBWKS-NXPQJCNCSA-N thymosin Chemical compound SC[C@@H](N)C(=O)N[C@H](CO)C(=O)N[C@H](CC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@H](C(C)C)C(=O)N[C@H](CC(O)=O)C(=O)N[C@H](C(C)C)C(=O)N[C@H](CO)C(=O)N[C@H](CO)C(=O)N[C@H](CCC(O)=O)C(=O)N[C@H]([C@@H](C)CC)C(=O)N[C@H]([C@H](C)O)C(=O)N[C@H](C(C)C)C(=O)N[C@H](CCCCN)C(=O)N[C@H](CC(O)=O)C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N[C@H](CCC(O)=O)C(=O)N[C@H](CCCCN)C(=O)N[C@H](CCCCN)C(=O)N[C@H](CCC(O)=O)C(=O)N[C@H](C(C)C)C(=O)N[C@H](C(C)C)C(=O)N[C@H](CCC(O)=O)C(=O)N[C@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@H](CCC(O)=O)C(O)=O LCJVIYPJPCBWKS-NXPQJCNCSA-N 0.000 description 1
229960000874 thyrotropin Drugs 0.000 description 1
230000001748 thyrotropin Effects 0.000 description 1
231100000331 toxic Toxicity 0.000 description 1
230000002588 toxic effect Effects 0.000 description 1
231100000041 toxicology testing Toxicity 0.000 description 1
230000032258 transport Effects 0.000 description 1
230000008733 trauma Effects 0.000 description 1
239000012588 trypsin Substances 0.000 description 1
208000001072 type 2 diabetes mellitus Diseases 0.000 description 1
GSXRBRIWJGAPDU-BBVRJQLQSA-N tyrocidine A Chemical class C([C@H]1C(=O)N[C@H](C(=O)N[C@@H](CCCN)C(=O)N[C@H](C(N[C@H](CC=2C=CC=CC=2)C(=O)N2CCC[C@H]2C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N1)=O)CC(C)C)C(C)C)C1=CC=C(O)C=C1 GSXRBRIWJGAPDU-BBVRJQLQSA-N 0.000 description 1
231100000397 ulcer Toxicity 0.000 description 1
241000712461 unidentified influenza virus Species 0.000 description 1
229960005486 vaccine Drugs 0.000 description 1
229960003726 vasopressin Drugs 0.000 description 1
238000005406 washing Methods 0.000 description 1
238000001262 western blot Methods 0.000 description 1
230000029663 wound healing Effects 0.000 description 1

Classifications

- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/19—Cytokines; Lymphokines; Interferons
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/62—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being a protein, peptide or polyamino acid

Landscapes

Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Medicinal Chemistry (AREA)
Veterinary Medicine (AREA)
Chemical & Material Sciences (AREA)
Engineering & Computer Science (AREA)
Bioinformatics & Cheminformatics (AREA)
Public Health (AREA)
General Health & Medical Sciences (AREA)
Pharmacology & Pharmacy (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Epidemiology (AREA)
Animal Behavior & Ethology (AREA)
Zoology (AREA)
Immunology (AREA)
Gastroenterology & Hepatology (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Medicinal Preparation (AREA)
Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)

CA002205771A 1997-05-22 1997-05-22 Administration amelioree pour traitement de fond Expired - Fee Related CA2205771C (fr)

Priority Applications (6)

Application Number	Priority Date	Filing Date	Title
CA002205771A CA2205771C (fr)	1997-05-22	1997-05-22	Administration amelioree pour traitement de fond
NZ501270A NZ501270A (en)	1997-05-22	1998-05-11	Pharmaceutical composition comprising hyaluronan (Mr less than 750,00) and a disease modifier (cytokine, a peptide mimicking a cytokine or a protein mimicking a cytokine) to enhance delivery of disease modifiers
PCT/CA1998/000448 WO1998052590A2 (fr)	1997-05-22	1998-05-11	Administration amelioree de modificateurs de pathologies
EP98920426A EP0998297A2 (fr)	1997-05-22	1998-05-11	Administration amelioree de modificateurs de pathologies
AU73286/98A AU740631B2 (en)	1997-05-22	1998-05-11	Improved delivery of disease modifiers
JP54972998A JP2001526666A (ja)	1997-05-22	1998-05-11	疾患調節薬の放出改良

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
CA002205771A CA2205771C (fr)	1997-05-22	1997-05-22	Administration amelioree pour traitement de fond

Publications (2)

Publication Number	Publication Date
CA2205771A1 CA2205771A1 (fr)	1998-11-22
CA2205771C true CA2205771C (fr)	2002-05-14

Family

ID=4160694

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
CA002205771A Expired - Fee Related CA2205771C (fr)	1997-05-22	1997-05-22	Administration amelioree pour traitement de fond

Country Status (6)

Country	Link
EP (1)	EP0998297A2 (fr)
JP (1)	JP2001526666A (fr)
AU (1)	AU740631B2 (fr)
CA (1)	CA2205771C (fr)
NZ (1)	NZ501270A (fr)
WO (1)	WO1998052590A2 (fr)

Families Citing this family (7)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US6875753B1 (en)	1996-03-14	2005-04-05	The Governors Of The University Of Alberta	Methods for cell mobilization using in vivo treatment with hyaluronan (HA)
US6960651B2 (en) *	1999-06-29	2005-11-01	Millennium Pharmaceuticals, Inc.	TANGO 332 polypeptides
CA2406593A1 (fr) *	2000-04-20	2001-11-01	Cangene Corporation	Conjugues peptidiques rhamm
AU2004242091C1 (en) *	2003-05-07	2009-12-24	La Jolla Institute For Molecular Medicine	Administration of hyaluronic acid to enhance the function of transplanted stem cells
DE102011122236A1 (de) *	2011-12-09	2013-06-13	Maria Clementine Martin Klosterfrau Vertriebsgesellschaft Mbh	Zusammensetzung für die topische Anwendung bei entzündlichen Erkrankungen der Haut und/oder Schleimhaut
FR3002452B1 (fr) *	2013-02-28	2016-02-12	Dermaconcept Jmc	Composition dermatologique antimicrobienne topique
PE20181363A1 (es)	2015-09-23	2018-08-27	Genentech Inc	Variantes optimizadas de anticuerpos anti-vegf

Family Cites Families (3)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CA1340994C (fr) *	1989-09-21	2000-05-16	Rudolf Edgar Dr. Falk	Traitement de maladies et d'etats pathologiques
GB9207949D0 (en) *	1992-04-09	1992-05-27	Univ Manitoba	Molecular cloning of a novel hyaluronan receptor that mediates tumor cell motility
AU3159595A (en) *	1994-08-30	1996-03-22	Hyal Pharmaceutical Corporation	Hyaluronic acid and derivatives for modulation of cellular activity

1997
- 1997-05-22 CA CA002205771A patent/CA2205771C/fr not_active Expired - Fee Related
1998
- 1998-05-11 AU AU73286/98A patent/AU740631B2/en not_active Ceased
- 1998-05-11 WO PCT/CA1998/000448 patent/WO1998052590A2/fr not_active Ceased
- 1998-05-11 JP JP54972998A patent/JP2001526666A/ja active Pending
- 1998-05-11 NZ NZ501270A patent/NZ501270A/en unknown
- 1998-05-11 EP EP98920426A patent/EP0998297A2/fr not_active Withdrawn

Also Published As

Publication number	Publication date
JP2001526666A (ja)	2001-12-18
WO1998052590A3 (fr)	1999-04-22
NZ501270A (en)	2001-08-31
AU7328698A (en)	1998-12-11
EP0998297A2 (fr)	2000-05-10
WO1998052590A2 (fr)	1998-11-26
AU740631B2 (en)	2001-11-08
CA2205771A1 (fr)	1998-11-22

Legal Events

Date	Code	Title	Description
1997-05-22	EEER	Examination request
2004-05-25	MKLA	Lapsed

Publication	Publication Date	Title
Holmskov et al.	1994	Collectins: collagenous C-type lectins of the innate immune defense system
US10040821B2 (en)	2018-08-07	Compositions containing HC-HA/PTX3 complexes and methods of use thereof
AU611856B2 (en)	1991-06-27	Stable pharmacuetical preparation containing granulocyte colony stimulating factor and process for producing the same
EP0401384B1 (fr)	1996-03-13	Facteur de stimulation de colonies de granulocytes modifies chimiquement
AU666007B2 (en)	1996-01-25	Protein formulation comprising growth hormone
JP2752206B2 (ja)	1998-05-18	顆粒球コロニー刺激因子を用いる粘膜炎の予防及び治療法
EP1129718A2 (fr)	2001-09-05	Utilisations thérapeutiques de produits protéiques augmentant le pouvoir bactéricide et/ou la perméabilité
RU94006023A (ru)	1996-04-20	Физиологически активная композиция на основе лиофилизированных модифицированных полиалкилен оксидом комплексов белка и полипептида с циклодекстрином и способ ее получения
CN103140499B (zh)	2014-12-17	一种粒细胞集落刺激因子与聚乙二醇的共轭物
CA2165727A1 (fr)	1996-09-17	Matrices de collagene liees par affinite, pour l'administration d'agents biologiquement actifs
JP2019523285A (ja)	2019-08-22	タンパク質およびペプチドの送達のための粒子
US8530417B2 (en)	2013-09-10	Y-shaped polyethylene glycol modified G-CSF, the preparation and use thereof
CA2205771C (fr)	2002-05-14	Administration amelioree pour traitement de fond
Wang et al.	2002	Characterization, stability, and formulations of basic fibroblast growth factor
AU2020281098B2 (en)	2024-05-02	Methods and compositions for treatment of cartilage damage and arthritis
US20110135624A1 (en)	2011-06-09	Therapeutic composition for autoimmune conditions
US8815812B2 (en)	2014-08-26	Synthetic arginine substituted peptides and their use
Gottschalk	1962	The relation between structure and function in some glycoproteins
EP0411033B1 (fr)	1994-09-07	Formulations stables pendant le stockage du m-csf dimerique homogene
KR930004598B1 (ko)	1993-06-01	단백질 수용액
EA031390B1 (ru)	2018-12-28	Система длительного высвобождения гидрофобных белков на основе амида гиалуроновой кислоты
Carter	1979	Glycosylation, intraspecies molecular heterogeneity and trans-species activity of mammalian interferons
CN117120460A (zh)	2023-11-24	分子超结构及其使用方法
JP2000143694A (ja)	2000-05-26	血小板由来白血球貪食能亢進因子の活性化因子
CA2878163C (fr)	2026-02-17	Compositions contenant des complexes hc-ah/ptx3 et procedes d'utilisation associes