ES2316154T3 - Peptidos cationicos antimicrobianos y procedimientos de seleccion de los mismos. - Google Patents

Peptidos cationicos antimicrobianos y procedimientos de seleccion de los mismos. Download PDF

Info

Publication number: ES2316154T3
Authority: ES; Spain
Prior art keywords: sub; baselineskip; peptide; seq; peptides
Prior art date: 1995-08-23
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 - Lifetime

Application number

ES96930303T

Other languages

English (en)

Spanish (es)

Inventor

Timothy J. Falla

Robert E. W. Hancock

Monisha Gough

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.)

University of British Columbia

Original Assignee

University of British Columbia

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.)

1995-08-23

Filing date

1996-08-23

Publication date

2009-04-01

1996-08-23 Application filed by University of British Columbia filed Critical University of British Columbia

2009-04-01 Application granted granted Critical

2009-04-01 Publication of ES2316154T3 publication Critical patent/ES2316154T3/es

2016-08-23 Anticipated expiration legal-status Critical

Status Expired - Lifetime legal-status Critical Current

Links

238000000034 method Methods 0.000 title claims abstract description 72
108010050820 Antimicrobial Cationic Peptides Proteins 0.000 title description 7
102000014133 Antimicrobial Cationic Peptides Human genes 0.000 title description 7
108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 351
150000001413 amino acids Chemical class 0.000 claims description 128
241000894006 Bacteria Species 0.000 claims description 48
108020004707 nucleic acids Proteins 0.000 claims description 43
150000007523 nucleic acids Chemical class 0.000 claims description 43
102000039446 nucleic acids Human genes 0.000 claims description 43
241000588724 Escherichia coli Species 0.000 claims description 24
230000003115 biocidal effect Effects 0.000 claims description 17
208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 16
230000012010 growth Effects 0.000 claims description 15
230000002401 inhibitory effect Effects 0.000 claims description 13
240000004808 Saccharomyces cerevisiae Species 0.000 claims description 11
208000035475 disorder Diseases 0.000 claims description 11
206010040047 Sepsis Diseases 0.000 claims description 10
241000222122 Candida albicans Species 0.000 claims description 8
208000037487 Endotoxemia Diseases 0.000 claims description 7
238000000338 in vitro Methods 0.000 claims description 7
241000293869 Salmonella enterica subsp. enterica serovar Typhimurium Species 0.000 claims description 6
108010093965 Polymyxin B Proteins 0.000 claims description 5
206010040070 Septic Shock Diseases 0.000 claims description 5
229920000024 polymyxin B Polymers 0.000 claims description 5
229960005266 polymyxin b Drugs 0.000 claims description 5
YJQPYGGHQPGBLI-UHFFFAOYSA-N Novobiocin Natural products O1C(C)(C)C(OC)C(OC(N)=O)C(O)C1OC1=CC=C(C(O)=C(NC(=O)C=2C=C(CC=C(C)C)C(O)=CC=2)C(=O)O2)C2=C1C YJQPYGGHQPGBLI-UHFFFAOYSA-N 0.000 claims description 4
241000191967 Staphylococcus aureus Species 0.000 claims description 4
229960002950 novobiocin Drugs 0.000 claims description 4
YJQPYGGHQPGBLI-KGSXXDOSSA-N novobiocin Chemical compound O1C(C)(C)[C@H](OC)[C@@H](OC(N)=O)[C@@H](O)[C@@H]1OC1=CC=C(C(O)=C(NC(=O)C=2C=C(CC=C(C)C)C(O)=CC=2)C(=O)O2)C2=C1C YJQPYGGHQPGBLI-KGSXXDOSSA-N 0.000 claims description 4
FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 3
229940095731 candida albicans Drugs 0.000 claims description 3
230000036303 septic shock Effects 0.000 claims description 3
150000003952 β-lactams Chemical class 0.000 claims description 3
239000003860 topical agent Substances 0.000 claims description 2
241000191963 Staphylococcus epidermidis Species 0.000 claims 2
230000005764 inhibitory process Effects 0.000 claims 2
102000004196 processed proteins & peptides Human genes 0.000 abstract description 134
125000002091 cationic group Chemical group 0.000 abstract description 62
230000000845 anti-microbial effect Effects 0.000 abstract description 54
QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 abstract description 16
QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 abstract description 16
COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 abstract description 10
ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 abstract description 9
COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 abstract description 9
KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 abstract description 8
239000004472 Lysine Substances 0.000 abstract description 8
239000004475 Arginine Substances 0.000 abstract description 6
ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 abstract description 6
FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 abstract description 5
229930182817 methionine Natural products 0.000 abstract description 5
ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 abstract description 4
KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 abstract description 4
ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 abstract description 3
OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 abstract description 3
KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 abstract description 3
ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 abstract description 3
229960000310 isoleucine Drugs 0.000 abstract description 3
AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 abstract description 3
OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 abstract description 3
239000004474 valine Substances 0.000 abstract description 3
ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 abstract description 2
AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 abstract description 2
KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 abstract description 2
235000001014 amino acid Nutrition 0.000 description 111
229940024606 amino acid Drugs 0.000 description 109
USSYUMHVHQSYNA-SLDJZXPVSA-N indolicidin Chemical compound CC[C@H](C)[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)N[C@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(N)=O)CC1=CNC2=CC=CC=C12 USSYUMHVHQSYNA-SLDJZXPVSA-N 0.000 description 70
210000004027 cell Anatomy 0.000 description 54
239000002158 endotoxin Substances 0.000 description 46
230000000694 effects Effects 0.000 description 42
229920006008 lipopolysaccharide Polymers 0.000 description 42
108060008682 Tumor Necrosis Factor Proteins 0.000 description 30
102000003390 tumor necrosis factor Human genes 0.000 description 30
108090000623 proteins and genes Proteins 0.000 description 28
108020004414 DNA Proteins 0.000 description 23
239000012528 membrane Substances 0.000 description 22
102000044503 Antimicrobial Peptides Human genes 0.000 description 21
108700042778 Antimicrobial Peptides Proteins 0.000 description 21
239000003242 anti bacterial agent Substances 0.000 description 19
102000004169 proteins and genes Human genes 0.000 description 19
238000012360 testing method Methods 0.000 description 19
QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 18
235000018102 proteins Nutrition 0.000 description 17
239000002609 medium Substances 0.000 description 16
229940088710 antibiotic agent Drugs 0.000 description 15
230000015572 biosynthetic process Effects 0.000 description 14
238000003786 synthesis reaction Methods 0.000 description 13
238000006243 chemical reaction Methods 0.000 description 12
239000013604 expression vector Substances 0.000 description 12
239000013615 primer Substances 0.000 description 12
230000002829 reductive effect Effects 0.000 description 12
239000004599 antimicrobial Substances 0.000 description 11
238000003556 assay Methods 0.000 description 11
230000004927 fusion Effects 0.000 description 11
239000002773 nucleotide Substances 0.000 description 11
125000003729 nucleotide group Chemical group 0.000 description 11
238000004458 analytical method Methods 0.000 description 10
238000002474 experimental method Methods 0.000 description 10
239000002502 liposome Substances 0.000 description 10
239000000047 product Substances 0.000 description 10
239000000243 solution Substances 0.000 description 10
241000699670 Mus sp. Species 0.000 description 9
108091028043 Nucleic acid sequence Proteins 0.000 description 9
238000010790 dilution Methods 0.000 description 9
239000012895 dilution Substances 0.000 description 9
238000001727 in vivo Methods 0.000 description 9
210000002540 macrophage Anatomy 0.000 description 9
238000006467 substitution reaction Methods 0.000 description 9
239000002253 acid Substances 0.000 description 8
239000003795 chemical substances by application Substances 0.000 description 8
210000003743 erythrocyte Anatomy 0.000 description 8
208000015181 infectious disease Diseases 0.000 description 8
239000013612 plasmid Substances 0.000 description 8
229920001184 polypeptide Polymers 0.000 description 8
239000003910 polypeptide antibiotic agent Substances 0.000 description 8
229960002429 proline Drugs 0.000 description 8
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 7
241000700605 Viruses Species 0.000 description 7
230000000844 anti-bacterial effect Effects 0.000 description 7
230000001965 increasing effect Effects 0.000 description 7
230000008823 permeabilization Effects 0.000 description 7
238000002360 preparation method Methods 0.000 description 7
125000006850 spacer group Chemical group 0.000 description 7
238000001228 spectrum Methods 0.000 description 7
239000000126 substance Substances 0.000 description 7
108091032973 (ribonucleotides)n+m Proteins 0.000 description 6
102000004190 Enzymes Human genes 0.000 description 6
108090000790 Enzymes Proteins 0.000 description 6
108091034117 Oligonucleotide Proteins 0.000 description 6
230000006870 function Effects 0.000 description 6
230000006698 induction Effects 0.000 description 6
238000002347 injection Methods 0.000 description 6
239000007924 injection Substances 0.000 description 6
239000000523 sample Substances 0.000 description 6
239000006228 supernatant Substances 0.000 description 6
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 6
239000006137 Luria-Bertani broth Substances 0.000 description 5
241001529936 Murinae Species 0.000 description 5
125000003275 alpha amino acid group Chemical group 0.000 description 5
230000001580 bacterial effect Effects 0.000 description 5
210000000170 cell membrane Anatomy 0.000 description 5
230000000295 complement effect Effects 0.000 description 5
150000001875 compounds Chemical class 0.000 description 5
201000010099 disease Diseases 0.000 description 5
238000004520 electroporation Methods 0.000 description 5
230000000813 microbial effect Effects 0.000 description 5
239000000203 mixture Substances 0.000 description 5
238000000746 purification Methods 0.000 description 5
239000003981 vehicle Substances 0.000 description 5
IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 4
230000006820 DNA synthesis Effects 0.000 description 4
108010002069 Defensins Proteins 0.000 description 4
102000000541 Defensins Human genes 0.000 description 4
241000233866 Fungi Species 0.000 description 4
108010070675 Glutathione transferase Proteins 0.000 description 4
102000005720 Glutathione transferase Human genes 0.000 description 4
239000000232 Lipid Bilayer Substances 0.000 description 4
108091005804 Peptidases Proteins 0.000 description 4
239000004365 Protease Substances 0.000 description 4
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 4
125000000129 anionic group Chemical group 0.000 description 4
210000004369 blood Anatomy 0.000 description 4
239000008280 blood Substances 0.000 description 4
238000004113 cell culture Methods 0.000 description 4
239000006285 cell suspension Substances 0.000 description 4
238000002983 circular dichroism Methods 0.000 description 4
238000003776 cleavage reaction Methods 0.000 description 4
239000002299 complementary DNA Substances 0.000 description 4
230000006378 damage Effects 0.000 description 4
230000003247 decreasing effect Effects 0.000 description 4
238000006073 displacement reaction Methods 0.000 description 4
239000012153 distilled water Substances 0.000 description 4
239000012634 fragment Substances 0.000 description 4
238000011534 incubation Methods 0.000 description 4
239000002054 inoculum Substances 0.000 description 4
238000007912 intraperitoneal administration Methods 0.000 description 4
150000002632 lipids Chemical class 0.000 description 4
BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 4
125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 4
-1 nucleotide triphosphates Chemical class 0.000 description 4
229920000642 polymer Polymers 0.000 description 4
238000006116 polymerization reaction Methods 0.000 description 4
239000003755 preservative agent Substances 0.000 description 4
125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 4
230000004044 response Effects 0.000 description 4
230000007017 scission Effects 0.000 description 4
238000000926 separation method Methods 0.000 description 4
239000007790 solid phase Substances 0.000 description 4
208000024891 symptom Diseases 0.000 description 4
108020004705 Codon Proteins 0.000 description 3
102000004594 DNA Polymerase I Human genes 0.000 description 3
108010017826 DNA Polymerase I Proteins 0.000 description 3
108010074860 Factor Xa Proteins 0.000 description 3
241000192125 Firmicutes Species 0.000 description 3
WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 3
WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 3
ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 3
108060004795 Methyltransferase Proteins 0.000 description 3
DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 3
102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 3
229920002684 Sepharose Polymers 0.000 description 3
230000001986 anti-endotoxic effect Effects 0.000 description 3
229940121375 antifungal agent Drugs 0.000 description 3
239000007864 aqueous solution Substances 0.000 description 3
239000003153 chemical reaction reagent Substances 0.000 description 3
ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 3
238000013461 design Methods 0.000 description 3
239000008121 dextrose Substances 0.000 description 3
239000000499 gel Substances 0.000 description 3
235000013922 glutamic acid Nutrition 0.000 description 3
239000004220 glutamic acid Substances 0.000 description 3
238000003780 insertion Methods 0.000 description 3
230000037431 insertion Effects 0.000 description 3
150000002500 ions Chemical class 0.000 description 3
231100001231 less toxic Toxicity 0.000 description 3
108020004999 messenger RNA Proteins 0.000 description 3
244000005700 microbiome Species 0.000 description 3
230000007935 neutral effect Effects 0.000 description 3
WTJKGGKOPKCXLL-RRHRGVEJSA-N phosphatidylcholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCCCCCCC=CCCCCCCCC WTJKGGKOPKCXLL-RRHRGVEJSA-N 0.000 description 3
230000003389 potentiating effect Effects 0.000 description 3
150000003839 salts Chemical class 0.000 description 3
239000011780 sodium chloride Substances 0.000 description 3
230000004083 survival effect Effects 0.000 description 3
239000000725 suspension Substances 0.000 description 3
238000013518 transcription Methods 0.000 description 3
230000035897 transcription Effects 0.000 description 3
239000013598 vector Substances 0.000 description 3
JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 2
MSWZFWKMSRAUBD-GASJEMHNSA-N 2-amino-2-deoxy-D-galactopyranose Chemical compound N[C@H]1C(O)O[C@H](CO)[C@H](O)[C@@H]1O MSWZFWKMSRAUBD-GASJEMHNSA-N 0.000 description 2
KUWPCJHYPSUOFW-YBXAARCKSA-N 2-nitrophenyl beta-D-galactoside Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1OC1=CC=CC=C1[N+]([O-])=O KUWPCJHYPSUOFW-YBXAARCKSA-N 0.000 description 2
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 2
DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 2
108050004290 Cecropin Proteins 0.000 description 2
CMSMOCZEIVJLDB-UHFFFAOYSA-N Cyclophosphamide Chemical compound ClCCN(CCCl)P1(=O)NCCCO1 CMSMOCZEIVJLDB-UHFFFAOYSA-N 0.000 description 2
102000053602 DNA Human genes 0.000 description 2
239000003155 DNA primer Substances 0.000 description 2
206010014824 Endotoxic shock Diseases 0.000 description 2
DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
206010019663 Hepatic failure Diseases 0.000 description 2
DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 2
TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
241000124008 Mammalia Species 0.000 description 2
241001465754 Metazoa Species 0.000 description 2
241000699666 Mus <mouse, genus> Species 0.000 description 2
108010055016 Rec A Recombinases Proteins 0.000 description 2
102000001218 Rec A Recombinases Human genes 0.000 description 2
GLNADSQYFUSGOU-GPTZEZBUSA-J Trypan blue Chemical compound [Na+].[Na+].[Na+].[Na+].C1=C(S([O-])(=O)=O)C=C2C=C(S([O-])(=O)=O)C(/N=N/C3=CC=C(C=C3C)C=3C=C(C(=CC=3)\N=N\C=3C(=CC4=CC(=CC(N)=C4C=3O)S([O-])(=O)=O)S([O-])(=O)=O)C)=C(O)C2=C1N GLNADSQYFUSGOU-GPTZEZBUSA-J 0.000 description 2
XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
RJURFGZVJUQBHK-UHFFFAOYSA-N actinomycin D Natural products CC1OC(=O)C(C(C)C)N(C)C(=O)CN(C)C(=O)C2CCCN2C(=O)C(C(C)C)NC(=O)C1NC(=O)C1=C(N)C(=O)C(C)=C2OC(C(C)=CC=C3C(=O)NC4C(=O)NC(C(N5CCCC5C(=O)N(C)CC(=O)N(C)C(C(C)C)C(=O)OC4C)=O)C(C)C)=C3N=C21 RJURFGZVJUQBHK-UHFFFAOYSA-N 0.000 description 2
239000000654 additive Substances 0.000 description 2
OIRDTQYFTABQOQ-KQYNXXCUSA-N adenosine Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O OIRDTQYFTABQOQ-KQYNXXCUSA-N 0.000 description 2
125000000539 amino acid group Chemical group 0.000 description 2
230000003321 amplification Effects 0.000 description 2
RDOXTESZEPMUJZ-UHFFFAOYSA-N anisole Chemical compound COC1=CC=CC=C1 RDOXTESZEPMUJZ-UHFFFAOYSA-N 0.000 description 2
239000003443 antiviral agent Substances 0.000 description 2
235000009582 asparagine Nutrition 0.000 description 2
229960001230 asparagine Drugs 0.000 description 2
MSWZFWKMSRAUBD-UHFFFAOYSA-N beta-D-galactosamine Natural products NC1C(O)OC(CO)C(O)C1O MSWZFWKMSRAUBD-UHFFFAOYSA-N 0.000 description 2
WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 2
230000037396 body weight Effects 0.000 description 2
MYSWGUAQZAJSOK-UHFFFAOYSA-N ciprofloxacin Chemical compound C12=CC(N3CCNCC3)=C(F)C=C2C(=O)C(C(=O)O)=CN1C1CC1 MYSWGUAQZAJSOK-UHFFFAOYSA-N 0.000 description 2
238000007796 conventional method Methods 0.000 description 2
229960004397 cyclophosphamide Drugs 0.000 description 2
230000009089 cytolysis Effects 0.000 description 2
OPTASPLRGRRNAP-UHFFFAOYSA-N cytosine Chemical compound NC=1C=CNC(=O)N=1 OPTASPLRGRRNAP-UHFFFAOYSA-N 0.000 description 2
230000034994 death Effects 0.000 description 2
239000005547 deoxyribonucleotide Substances 0.000 description 2
229940079593 drug Drugs 0.000 description 2
239000003814 drug Substances 0.000 description 2
239000000839 emulsion Substances 0.000 description 2
238000005516 engineering process Methods 0.000 description 2
230000032050 esterification Effects 0.000 description 2
238000005886 esterification reaction Methods 0.000 description 2
210000003527 eukaryotic cell Anatomy 0.000 description 2
239000000284 extract Substances 0.000 description 2
238000001914 filtration Methods 0.000 description 2
238000002509 fluorescent in situ hybridization Methods 0.000 description 2
235000019253 formic acid Nutrition 0.000 description 2
238000004108 freeze drying Methods 0.000 description 2
108020001507 fusion proteins Proteins 0.000 description 2
102000037865 fusion proteins Human genes 0.000 description 2
230000002068 genetic effect Effects 0.000 description 2
ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 2
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 2
UYTPUPDQBNUYGX-UHFFFAOYSA-N guanine Chemical compound O=C1NC(N)=NC2=C1N=CN2 UYTPUPDQBNUYGX-UHFFFAOYSA-N 0.000 description 2
230000002209 hydrophobic effect Effects 0.000 description 2
125000001165 hydrophobic group Chemical group 0.000 description 2
239000003112 inhibitor Substances 0.000 description 2
235000014705 isoleucine Nutrition 0.000 description 2
235000005772 leucine Nutrition 0.000 description 2
239000007788 liquid Substances 0.000 description 2
208000007903 liver failure Diseases 0.000 description 2
231100000835 liver failure Toxicity 0.000 description 2
238000004519 manufacturing process Methods 0.000 description 2
OVHQWOXKMOVDJP-UHFFFAOYSA-N melitin Chemical compound OC1C(O)C(O)C(C)OC1OC1C(O)C(OC=2C=C3C(C(C(OC4C(C(O)C(O)C(COC5C(C(O)C(O)C(CO)O5)O)O4)O)=C(C=4C=CC(O)=CC=4)O3)=O)=C(O)C=2)OC(C)C1O OVHQWOXKMOVDJP-UHFFFAOYSA-N 0.000 description 2
150000004702 methyl esters Chemical class 0.000 description 2
230000004048 modification Effects 0.000 description 2
238000012986 modification Methods 0.000 description 2
230000035772 mutation Effects 0.000 description 2
229910052757 nitrogen Inorganic materials 0.000 description 2
238000003199 nucleic acid amplification method Methods 0.000 description 2
238000010647 peptide synthesis reaction Methods 0.000 description 2
239000012985 polymerization agent Substances 0.000 description 2
230000035755 proliferation Effects 0.000 description 2
230000012743 protein tagging Effects 0.000 description 2
108091008146 restriction endonucleases Proteins 0.000 description 2
238000010839 reverse transcription Methods 0.000 description 2
230000002441 reversible effect Effects 0.000 description 2
FGDZQCVHDSGLHJ-UHFFFAOYSA-M rubidium chloride Chemical compound [Cl-].[Rb+] FGDZQCVHDSGLHJ-UHFFFAOYSA-M 0.000 description 2
210000002966 serum Anatomy 0.000 description 2
241000894007 species Species 0.000 description 2
238000012916 structural analysis Methods 0.000 description 2
230000002195 synergetic effect Effects 0.000 description 2
238000002560 therapeutic procedure Methods 0.000 description 2
RWQNBRDOKXIBIV-UHFFFAOYSA-N thymine Chemical compound CC1=CNC(=O)NC1=O RWQNBRDOKXIBIV-UHFFFAOYSA-N 0.000 description 2
231100000331 toxic Toxicity 0.000 description 2
230000002588 toxic effect Effects 0.000 description 2
231100000419 toxicity Toxicity 0.000 description 2
230000001988 toxicity Effects 0.000 description 2
238000001890 transfection Methods 0.000 description 2
230000009466 transformation Effects 0.000 description 2
239000001226 triphosphate Substances 0.000 description 2
235000011178 triphosphate Nutrition 0.000 description 2
230000006433 tumor necrosis factor production Effects 0.000 description 2
235000014393 valine Nutrition 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
125000003088 (fluoren-9-ylmethoxy)carbonyl group Chemical group 0.000 description 1
TZCPCKNHXULUIY-RGULYWFUSA-N 1,2-distearoyl-sn-glycero-3-phosphoserine Chemical compound CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(O)(=O)OC[C@H](N)C(O)=O)OC(=O)CCCCCCCCCCCCCCCCC TZCPCKNHXULUIY-RGULYWFUSA-N 0.000 description 1
WTJKGGKOPKCXLL-VYOBOKEXSA-N 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCCCCCC\C=C/CCCCCCCC WTJKGGKOPKCXLL-VYOBOKEXSA-N 0.000 description 1
PAZGBAOHGQRCBP-DDDNOICHSA-N 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP(O)(=O)OCC(O)CO)OC(=O)CCCCCCC\C=C/CCCCCCCC PAZGBAOHGQRCBP-DDDNOICHSA-N 0.000 description 1
CJNZAXGUTKBIHP-UHFFFAOYSA-N 2-iodobenzoic acid Chemical compound OC(=O)C1=CC=CC=C1I CJNZAXGUTKBIHP-UHFFFAOYSA-N 0.000 description 1
NKDFYOWSKOHCCO-YPVLXUMRSA-N 20-hydroxyecdysone Chemical compound C1[C@@H](O)[C@@H](O)C[C@]2(C)[C@@H](CC[C@@]3([C@@H]([C@@](C)(O)[C@H](O)CCC(C)(O)C)CC[C@]33O)C)C3=CC(=O)[C@@H]21 NKDFYOWSKOHCCO-YPVLXUMRSA-N 0.000 description 1
108010068327 4-hydroxyphenylpyruvate dioxygenase Proteins 0.000 description 1
206010001052 Acute respiratory distress syndrome Diseases 0.000 description 1
229920000936 Agarose Polymers 0.000 description 1
108700028369 Alleles Proteins 0.000 description 1
101710150620 Anionic peptide Proteins 0.000 description 1
206010004053 Bacterial toxaemia Diseases 0.000 description 1
102100026189 Beta-galactosidase Human genes 0.000 description 1
241000283690 Bos taurus Species 0.000 description 1
108091003079 Bovine Serum Albumin Proteins 0.000 description 1
239000002126 C01EB10 - Adenosine Substances 0.000 description 1
UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
241000893640 Carcharhinus longimanus Species 0.000 description 1
206010061005 Cardiac myxoma Diseases 0.000 description 1
102000014914 Carrier Proteins Human genes 0.000 description 1
108010078791 Carrier Proteins Proteins 0.000 description 1
208000005024 Castleman disease Diseases 0.000 description 1
229930186147 Cephalosporin Natural products 0.000 description 1
VEXZGXHMUGYJMC-UHFFFAOYSA-M Chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 0.000 description 1
108091026890 Coding region Proteins 0.000 description 1
102000004127 Cytokines Human genes 0.000 description 1
108090000695 Cytokines Proteins 0.000 description 1
108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
108010092160 Dactinomycin Proteins 0.000 description 1
238000002965 ELISA Methods 0.000 description 1
LVGKNOAMLMIIKO-UHFFFAOYSA-N Elaidinsaeure-aethylester Natural products CCCCCCCCC=CCCCCCCCC(=O)OCC LVGKNOAMLMIIKO-UHFFFAOYSA-N 0.000 description 1
102100031780 Endonuclease Human genes 0.000 description 1
241000588697 Enterobacter cloacae Species 0.000 description 1
241000620209 Escherichia coli DH5[alpha] Species 0.000 description 1
CEAZRRDELHUEMR-URQXQFDESA-N Gentamicin Chemical compound O1[C@H](C(C)NC)CC[C@@H](N)[C@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](NC)[C@@](C)(O)CO2)O)[C@H](N)C[C@@H]1N CEAZRRDELHUEMR-URQXQFDESA-N 0.000 description 1
229930182566 Gentamicin Natural products 0.000 description 1
108010024636 Glutathione Proteins 0.000 description 1
239000004471 Glycine Substances 0.000 description 1
208000023329 Gun shot wound Diseases 0.000 description 1
239000007995 HEPES buffer Substances 0.000 description 1
208000031886 HIV Infections Diseases 0.000 description 1
208000002250 Hematologic Neoplasms Diseases 0.000 description 1
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 1
241000238631 Hexapoda Species 0.000 description 1
241000282412 Homo Species 0.000 description 1
208000001953 Hypotension Diseases 0.000 description 1
DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
239000007836 KH2PO4 Substances 0.000 description 1
XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
229930182816 L-glutamine Natural products 0.000 description 1
LRQKBLKVPFOOQJ-YFKPBYRVSA-N L-norleucine Chemical compound CCCC[C@H]([NH3+])C([O-])=O LRQKBLKVPFOOQJ-YFKPBYRVSA-N 0.000 description 1
AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
108060003100 Magainin Proteins 0.000 description 1
102000018697 Membrane Proteins Human genes 0.000 description 1
108010052285 Membrane Proteins Proteins 0.000 description 1
201000009906 Meningitis Diseases 0.000 description 1
208000034578 Multiple myelomas Diseases 0.000 description 1
241000588653 Neisseria Species 0.000 description 1
206010028980 Neoplasm Diseases 0.000 description 1
108020005187 Oligonucleotide Probes Proteins 0.000 description 1
206010053159 Organ failure Diseases 0.000 description 1
229930182555 Penicillin Natural products 0.000 description 1
102000035195 Peptidases Human genes 0.000 description 1
108010067902 Peptide Library Proteins 0.000 description 1
206010035226 Plasma cell myeloma Diseases 0.000 description 1
239000002202 Polyethylene glycol Substances 0.000 description 1
241000589516 Pseudomonas Species 0.000 description 1
241000589517 Pseudomonas aeruginosa Species 0.000 description 1
206010037660 Pyrexia Diseases 0.000 description 1
108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
108020004511 Recombinant DNA Proteins 0.000 description 1
208000001647 Renal Insufficiency Diseases 0.000 description 1
208000013616 Respiratory Distress Syndrome Diseases 0.000 description 1
108091028664 Ribonucleotide Proteins 0.000 description 1
241000607142 Salmonella Species 0.000 description 1
206010070834 Sensitisation Diseases 0.000 description 1
229920005654 Sephadex Polymers 0.000 description 1
239000012507 Sephadex™ Substances 0.000 description 1
MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
241000607768 Shigella Species 0.000 description 1
241000295644 Staphylococcaceae Species 0.000 description 1
241000191940 Staphylococcus Species 0.000 description 1
101000582398 Staphylococcus aureus Replication initiation protein Proteins 0.000 description 1
241000194017 Streptococcus Species 0.000 description 1
210000001744 T-lymphocyte Anatomy 0.000 description 1
239000004809 Teflon Substances 0.000 description 1
229920006362 Teflon® Polymers 0.000 description 1
AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
239000004473 Threonine Substances 0.000 description 1
208000013222 Toxemia Diseases 0.000 description 1
241000607734 Yersinia <bacteria> Species 0.000 description 1
238000002835 absorbance Methods 0.000 description 1
238000004847 absorption spectroscopy Methods 0.000 description 1
150000007513 acids Chemical class 0.000 description 1
RJURFGZVJUQBHK-IIXSONLDSA-N actinomycin D Chemical compound C[C@H]1OC(=O)[C@H](C(C)C)N(C)C(=O)CN(C)C(=O)[C@@H]2CCCN2C(=O)[C@@H](C(C)C)NC(=O)[C@H]1NC(=O)C1=C(N)C(=O)C(C)=C2OC(C(C)=CC=C3C(=O)N[C@@H]4C(=O)N[C@@H](C(N5CCC[C@H]5C(=O)N(C)CC(=O)N(C)[C@@H](C(C)C)C(=O)O[C@@H]4C)=O)C(C)C)=C3N=C21 RJURFGZVJUQBHK-IIXSONLDSA-N 0.000 description 1
230000009471 action Effects 0.000 description 1
230000000996 additive effect Effects 0.000 description 1
229960005305 adenosine Drugs 0.000 description 1
201000000028 adult respiratory distress syndrome Diseases 0.000 description 1
239000000443 aerosol Substances 0.000 description 1
239000011543 agarose gel Substances 0.000 description 1
235000004279 alanine Nutrition 0.000 description 1
230000001476 alcoholic effect Effects 0.000 description 1
150000001412 amines Chemical class 0.000 description 1
229940126575 aminoglycoside Drugs 0.000 description 1
239000005557 antagonist Substances 0.000 description 1
230000000843 anti-fungal effect Effects 0.000 description 1
230000000259 anti-tumor effect Effects 0.000 description 1
230000000840 anti-viral effect Effects 0.000 description 1
239000003429 antifungal agent Substances 0.000 description 1
238000012458 antifungal assay Methods 0.000 description 1
238000002802 antimicrobial activity assay Methods 0.000 description 1
239000002246 antineoplastic agent Substances 0.000 description 1
239000003963 antioxidant agent Substances 0.000 description 1
239000003125 aqueous solvent Substances 0.000 description 1
235000003704 aspartic acid Nutrition 0.000 description 1
208000022362 bacterial infectious disease Diseases 0.000 description 1
230000003385 bacteriostatic effect Effects 0.000 description 1
230000009286 beneficial effect Effects 0.000 description 1
230000008901 benefit Effects 0.000 description 1
108010005774 beta-Galactosidase Proteins 0.000 description 1
OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
239000000872 buffer Substances 0.000 description 1
239000007975 buffered saline Substances 0.000 description 1
210000004899 c-terminal region Anatomy 0.000 description 1
239000001110 calcium chloride Substances 0.000 description 1
229910001628 calcium chloride Inorganic materials 0.000 description 1
235000011148 calcium chloride Nutrition 0.000 description 1
238000004364 calculation method Methods 0.000 description 1
229940075397 calomel Drugs 0.000 description 1
239000004202 carbamide Substances 0.000 description 1
239000000969 carrier Substances 0.000 description 1
230000015556 catabolic process Effects 0.000 description 1
150000001768 cations Chemical class 0.000 description 1
HVFLCNVBZFFHBT-ZKDACBOMSA-N cefepime Chemical compound S([C@@H]1[C@@H](C(N1C=1C([O-])=O)=O)NC(=O)\C(=N/OC)C=2N=C(N)SC=2)CC=1C[N+]1(C)CCCC1 HVFLCNVBZFFHBT-ZKDACBOMSA-N 0.000 description 1
229960002100 cefepime Drugs 0.000 description 1
ORFOPKXBNMVMKC-DWVKKRMSSA-N ceftazidime Chemical compound S([C@@H]1[C@@H](C(N1C=1C([O-])=O)=O)NC(=O)\C(=N/OC(C)(C)C(O)=O)C=2N=C(N)SC=2)CC=1C[N+]1=CC=CC=C1 ORFOPKXBNMVMKC-DWVKKRMSSA-N 0.000 description 1
229960000484 ceftazidime Drugs 0.000 description 1
230000006037 cell lysis Effects 0.000 description 1
230000001413 cellular effect Effects 0.000 description 1
238000005119 centrifugation Methods 0.000 description 1
229940124587 cephalosporin Drugs 0.000 description 1
150000001780 cephalosporins Chemical class 0.000 description 1
230000008859 change Effects 0.000 description 1
238000012512 characterization method Methods 0.000 description 1
239000002738 chelating agent Substances 0.000 description 1
229960005091 chloramphenicol Drugs 0.000 description 1
WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
238000013375 chromatographic separation Methods 0.000 description 1
229960003405 ciprofloxacin Drugs 0.000 description 1
238000010367 cloning Methods 0.000 description 1
239000000356 contaminant Substances 0.000 description 1
238000011109 contamination Methods 0.000 description 1
238000001816 cooling Methods 0.000 description 1
239000013256 coordination polymer Substances 0.000 description 1
229920001577 copolymer Chemical compound 0.000 description 1
239000002537 cosmetic Substances 0.000 description 1
239000013058 crude material Substances 0.000 description 1
210000004748 cultured cell Anatomy 0.000 description 1
XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
235000018417 cysteine Nutrition 0.000 description 1
229940104302 cytosine Drugs 0.000 description 1
230000001086 cytosolic effect Effects 0.000 description 1
231100000433 cytotoxic Toxicity 0.000 description 1
230000001472 cytotoxic effect Effects 0.000 description 1
SUYVUBYJARFZHO-RRKCRQDMSA-N dATP Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-RRKCRQDMSA-N 0.000 description 1
SUYVUBYJARFZHO-UHFFFAOYSA-N dATP Natural products C1=NC=2C(N)=NC=NC=2N1C1CC(O)C(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-UHFFFAOYSA-N 0.000 description 1
RGWHQCVHVJXOKC-SHYZEUOFSA-J dCTP(4-) Chemical compound O=C1N=C(N)C=CN1[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)C1 RGWHQCVHVJXOKC-SHYZEUOFSA-J 0.000 description 1
HAAZLUGHYHWQIW-KVQBGUIXSA-N dGTP Chemical compound C1=NC=2C(=O)NC(N)=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 HAAZLUGHYHWQIW-KVQBGUIXSA-N 0.000 description 1
229960000640 dactinomycin Drugs 0.000 description 1
125000001295 dansyl group Chemical group [H]C1=C([H])C(N(C([H])([H])[H])C([H])([H])[H])=C2C([H])=C([H])C([H])=C(C2=C1[H])S(*)(=O)=O 0.000 description 1
DIOQZVSQGTUSAI-UHFFFAOYSA-N decane Chemical compound CCCCCCCCCC DIOQZVSQGTUSAI-UHFFFAOYSA-N 0.000 description 1
230000008260 defense mechanism Effects 0.000 description 1
230000002950 deficient Effects 0.000 description 1
238000006731 degradation reaction Methods 0.000 description 1
238000004925 denaturation Methods 0.000 description 1
230000036425 denaturation Effects 0.000 description 1
125000002637 deoxyribonucleotide group Chemical group 0.000 description 1
230000001419 dependent effect Effects 0.000 description 1
230000029087 digestion Effects 0.000 description 1
ZOMNIUBKTOKEHS-UHFFFAOYSA-L dimercury dichloride Chemical compound Cl[Hg][Hg]Cl ZOMNIUBKTOKEHS-UHFFFAOYSA-L 0.000 description 1
LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
208000009190 disseminated intravascular coagulation Diseases 0.000 description 1
238000009510 drug design Methods 0.000 description 1
230000009982 effect on human Effects 0.000 description 1
239000003792 electrolyte Substances 0.000 description 1
238000005538 encapsulation Methods 0.000 description 1
230000002255 enzymatic effect Effects 0.000 description 1
LVGKNOAMLMIIKO-QXMHVHEDSA-N ethyl oleate Chemical compound CCCCCCCC\C=C/CCCCCCCC(=O)OCC LVGKNOAMLMIIKO-QXMHVHEDSA-N 0.000 description 1
229940093471 ethyl oleate Drugs 0.000 description 1
230000007717 exclusion Effects 0.000 description 1
239000012091 fetal bovine serum Substances 0.000 description 1
210000002950 fibroblast Anatomy 0.000 description 1
238000011049 filling Methods 0.000 description 1
239000012530 fluid Substances 0.000 description 1
235000013305 food Nutrition 0.000 description 1
235000013373 food additive Nutrition 0.000 description 1
239000002778 food additive Substances 0.000 description 1
238000010230 functional analysis Methods 0.000 description 1
239000007789 gas Substances 0.000 description 1
238000002523 gelfiltration Methods 0.000 description 1
229960002518 gentamicin Drugs 0.000 description 1
229960003180 glutathione Drugs 0.000 description 1
239000008187 granular material Substances 0.000 description 1
238000010438 heat treatment Methods 0.000 description 1
229960002897 heparin Drugs 0.000 description 1
229920000669 heparin Polymers 0.000 description 1
238000011141 high resolution liquid chromatography Methods 0.000 description 1
210000005260 human cell Anatomy 0.000 description 1
238000009396 hybridization Methods 0.000 description 1
230000007062 hydrolysis Effects 0.000 description 1
238000006460 hydrolysis reaction Methods 0.000 description 1
230000036543 hypotension Effects 0.000 description 1
230000001900 immune effect Effects 0.000 description 1
230000001506 immunosuppresive effect Effects 0.000 description 1
230000006872 improvement Effects 0.000 description 1
238000010348 incorporation Methods 0.000 description 1
230000001939 inductive effect Effects 0.000 description 1
230000002757 inflammatory effect Effects 0.000 description 1
208000037798 influenza B Diseases 0.000 description 1
238000001802 infusion Methods 0.000 description 1
208000014674 injury Diseases 0.000 description 1
230000003993 interaction Effects 0.000 description 1
238000001990 intravenous administration Methods 0.000 description 1
238000002955 isolation Methods 0.000 description 1
125000000741 isoleucyl group Chemical group [H]N([H])C(C(C([H])([H])[H])C([H])([H])C([H])([H])[H])C(=O)O* 0.000 description 1
238000005304 joining Methods 0.000 description 1
210000003734 kidney Anatomy 0.000 description 1
201000006370 kidney failure Diseases 0.000 description 1
108010060845 lactose permease Proteins 0.000 description 1
230000003902 lesion Effects 0.000 description 1
230000001665 lethal effect Effects 0.000 description 1
210000000265 leukocyte Anatomy 0.000 description 1
201000002364 leukopenia Diseases 0.000 description 1
231100001022 leukopenia Toxicity 0.000 description 1
238000001638 lipofection Methods 0.000 description 1
238000009630 liquid culture Methods 0.000 description 1
210000004072 lung Anatomy 0.000 description 1
235000010335 lysozyme Nutrition 0.000 description 1
229910001629 magnesium chloride Inorganic materials 0.000 description 1
239000000463 material Substances 0.000 description 1
238000005259 measurement Methods 0.000 description 1
230000007246 mechanism Effects 0.000 description 1
230000028161 membrane depolarization Effects 0.000 description 1
UZKWTJUDCOPSNM-UHFFFAOYSA-N methoxybenzene Substances CCCCOC=C UZKWTJUDCOPSNM-UHFFFAOYSA-N 0.000 description 1
244000000010 microbial pathogen Species 0.000 description 1
238000000520 microinjection Methods 0.000 description 1
239000004005 microsphere Substances 0.000 description 1
229910000402 monopotassium phosphate Inorganic materials 0.000 description 1
235000019796 monopotassium phosphate Nutrition 0.000 description 1
230000021332 multicellular organism growth Effects 0.000 description 1
208000004235 neutropenia Diseases 0.000 description 1
210000000440 neutrophil Anatomy 0.000 description 1
239000000346 nonvolatile oil Substances 0.000 description 1
235000015097 nutrients Nutrition 0.000 description 1
239000002751 oligonucleotide probe Substances 0.000 description 1
239000004006 olive oil Substances 0.000 description 1
235000008390 olive oil Nutrition 0.000 description 1
150000002895 organic esters Chemical class 0.000 description 1
238000007911 parenteral administration Methods 0.000 description 1
230000008506 pathogenesis Effects 0.000 description 1
239000008188 pellet Substances 0.000 description 1
150000002960 penicillins Chemical class 0.000 description 1
239000002953 phosphate buffered saline Substances 0.000 description 1
230000008288 physiological mechanism Effects 0.000 description 1
231100000614 poison Toxicity 0.000 description 1
239000002574 poison Substances 0.000 description 1
231100000572 poisoning Toxicity 0.000 description 1
230000000607 poisoning effect Effects 0.000 description 1
229920001223 polyethylene glycol Polymers 0.000 description 1
238000003752 polymerase chain reaction Methods 0.000 description 1
GNSKLFRGEWLPPA-UHFFFAOYSA-M potassium dihydrogen phosphate Chemical compound [K+].OP(O)([O-])=O GNSKLFRGEWLPPA-UHFFFAOYSA-M 0.000 description 1
230000036515 potency Effects 0.000 description 1
239000002987 primer (paints) Substances 0.000 description 1
230000008569 process Effects 0.000 description 1
210000001236 prokaryotic cell Anatomy 0.000 description 1
238000001742 protein purification Methods 0.000 description 1
238000001243 protein synthesis Methods 0.000 description 1
230000006337 proteolytic cleavage Effects 0.000 description 1
210000001938 protoplast Anatomy 0.000 description 1
150000007660 quinolones Chemical class 0.000 description 1
230000009257 reactivity Effects 0.000 description 1
230000009467 reduction Effects 0.000 description 1
235000021067 refined food Nutrition 0.000 description 1
230000010076 replication Effects 0.000 description 1
239000002336 ribonucleotide Substances 0.000 description 1
125000002652 ribonucleotide group Chemical group 0.000 description 1
229920006395 saturated elastomer Polymers 0.000 description 1
239000013049 sediment Substances 0.000 description 1
238000010187 selection method Methods 0.000 description 1
230000008313 sensitization Effects 0.000 description 1
208000013223 septicemia Diseases 0.000 description 1
238000012163 sequencing technique Methods 0.000 description 1
238000013207 serial dilution Methods 0.000 description 1
230000035939 shock Effects 0.000 description 1
RYMZZMVNJRMUDD-HGQWONQESA-N simvastatin Chemical compound C([C@H]1[C@@H](C)C=CC2=C[C@H](C)C[C@@H]([C@H]12)OC(=O)C(C)(C)CC)C[C@@H]1C[C@@H](O)CC(=O)O1 RYMZZMVNJRMUDD-HGQWONQESA-N 0.000 description 1
238000002741 site-directed mutagenesis Methods 0.000 description 1
229910052708 sodium Inorganic materials 0.000 description 1
239000011734 sodium Substances 0.000 description 1
239000012064 sodium phosphate buffer Substances 0.000 description 1
239000007787 solid Substances 0.000 description 1
239000002904 solvent Substances 0.000 description 1
238000009331 sowing Methods 0.000 description 1
239000000758 substrate Substances 0.000 description 1
230000009885 systemic effect Effects 0.000 description 1
238000011285 therapeutic regimen Methods 0.000 description 1
238000004809 thin layer chromatography Methods 0.000 description 1
206010043554 thrombocytopenia Diseases 0.000 description 1
229940113082 thymine Drugs 0.000 description 1
239000003053 toxin Substances 0.000 description 1
231100000765 toxin Toxicity 0.000 description 1
108700012359 toxins Proteins 0.000 description 1
230000001131 transforming effect Effects 0.000 description 1
230000014616 translation Effects 0.000 description 1
230000008733 trauma Effects 0.000 description 1
125000002264 triphosphate group Chemical class [H]OP(=O)(O[H])OP(=O)(O[H])OP(=O)(O[H])O* 0.000 description 1
229940046728 tumor necrosis factor alpha inhibitor Drugs 0.000 description 1
239000002451 tumor necrosis factor inhibitor Substances 0.000 description 1
235000015112 vegetable and seed oil Nutrition 0.000 description 1
239000008158 vegetable oil Substances 0.000 description 1
230000035899 viability Effects 0.000 description 1
230000003612 virological effect Effects 0.000 description 1
238000005406 washing Methods 0.000 description 1
239000002699 waste material Substances 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/02—Local antiseptics
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/10—Antimycotics
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4723—Cationic antimicrobial peptides, e.g. defensins
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/08—Linear peptides containing only normal peptide links having 12 to 20 amino acids
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A50/00—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE in human health protection, e.g. against extreme weather
- Y02A50/30—Against vector-borne diseases, e.g. mosquito-borne, fly-borne, tick-borne or waterborne diseases whose impact is exacerbated by climate change

Landscapes

Chemical & Material Sciences (AREA)
Health & Medical Sciences (AREA)
Organic Chemistry (AREA)
Life Sciences & Earth Sciences (AREA)
General Health & Medical Sciences (AREA)
Medicinal Chemistry (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Molecular Biology (AREA)
Genetics & Genomics (AREA)
Biophysics (AREA)
Biochemistry (AREA)
Veterinary Medicine (AREA)
Animal Behavior & Ethology (AREA)
Public Health (AREA)
Pharmacology & Pharmacy (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
General Chemical & Material Sciences (AREA)
Chemical Kinetics & Catalysis (AREA)
Oncology (AREA)
Communicable Diseases (AREA)
Toxicology (AREA)
Zoology (AREA)
Gastroenterology & Hepatology (AREA)
Peptides Or Proteins (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
Agricultural Chemicals And Associated Chemicals (AREA)

ES96930303T 1995-08-23 1996-08-23 Peptidos cationicos antimicrobianos y procedimientos de seleccion de los mismos. Expired - Lifetime ES2316154T3 (es)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
US268795P	1995-08-23	1995-08-23
US2687P		1995-08-23

Publications (1)

Publication Number	Publication Date
ES2316154T3 true ES2316154T3 (es)	2009-04-01

Family

ID=21701983

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
ES96930303T Expired - Lifetime ES2316154T3 (es)	1995-08-23	1996-08-23	Peptidos cationicos antimicrobianos y procedimientos de seleccion de los mismos.

Country Status (9)

Country	Link
US (2)	US6191254B1 (2)
EP (1)	EP0846128B1 (2)
JP (1)	JP3860838B2 (2)
AT (1)	ATE412668T1 (2)
AU (1)	AU6940796A (2)
CA (1)	CA2230160A1 (2)
DE (1)	DE69637731D1 (2)
ES (1)	ES2316154T3 (2)
WO (1)	WO1997008199A2 (2)

Families Citing this family (53)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US6180604B1 (en)	1996-08-21	2001-01-30	Micrologix Biotech Inc.	Compositions and methods for treating infections using analogues of indolicidin
EP1174439B1 (en) *	1996-08-21	2008-10-08	Migenix Inc.	Compositions and methods for treating infections using analogues of indolicidin
US6503881B2 (en) *	1996-08-21	2003-01-07	Micrologix Biotech Inc.	Compositions and methods for treating infections using cationic peptides alone or in combination with antibiotics
US6303575B1 (en) *	1998-05-12	2001-10-16	The Regents Of The University Of California	Indolicidin analogs and methods of using same
US6444645B1 (en)	1998-06-18	2002-09-03	The Regents Of The University Of California	Crosslink-stabilized indolicidin analogs
US6288212B1 (en) *	1998-08-28	2001-09-11	The University Of British Columbia	Anti-endotoxic, antimicrobial cationic peptides and methods of use therefor
WO2000026344A1 (en) *	1998-10-30	2000-05-11	Interlink Biotechnologies Llc	Peptides with enhanced stability to protease degradation
US6946261B1 (en)	1998-11-20	2005-09-20	Migenix Inc.	Efficient methods for producing anti-microbial cationic peptides in host cells
US6335318B1 (en)	1999-05-10	2002-01-01	The Regents Of The University Of California	Antimicrobial theta defensins and methods of using same
US6497676B1 (en)	2000-02-10	2002-12-24	Baxter International	Method and apparatus for monitoring and controlling peritoneal dialysis therapy
US6337317B1 (en) *	2000-06-27	2002-01-08	The University Of British Columbia	Antimicrobial peptides and methods of use thereof
US6835536B2 (en)	2001-08-21	2004-12-28	Micrologix Biotech Inc.	Antimicrobial cationic peptides and formulations thereof
US8933029B2 (en) *	2001-08-24	2015-01-13	Carrus Capital Corporation	Antimicrobial and anti-inflammatory peptides
KR100438416B1 (ko) *	2001-09-19	2004-07-02	학교법인조선대학교	Ｃａ－ｍａ 펩타이드의 아미노산 중 하나 또는 그 이상을치환하여 ＋ 전극과 소수성 영역이 증가된 신규한펩타이드 및 그를 포함하는 약학적 조성물
US7507787B2 (en) *	2001-12-03	2009-03-24	The University Of British Columbia	Effectors of innate immunity
US20030125662A1 (en) *	2002-01-03	2003-07-03	Tuan Bui	Method and apparatus for providing medical treatment therapy based on calculated demand
US20030219854A1 (en) *	2002-03-21	2003-11-27	Micrologix Biotech Inc.	Methods for producing modified anti-infective peptides
AU2003231471A1 (en) *	2002-04-25	2003-11-10	Toagosei Co., Ltd.	Antimicrobial polypeptide and utizliation thereof
US7119070B2 (en)	2002-04-30	2006-10-10	The Regents Of The University Of California	Antimicrobial theta defensins, analogs thereof, and methods of use
US7033769B2 (en) *	2002-05-23	2006-04-25	The United States Of America As Represented By The Secretary Of The Army	Method for discovering one or more peptides adapted for specific binding to a microorganism of interest
US7238164B2 (en)	2002-07-19	2007-07-03	Baxter International Inc.	Systems, methods and apparatuses for pumping cassette-based therapies
US7550430B2 (en) *	2003-08-18	2009-06-23	E.I. Du Pont De Nemours And Company	Cationic antimicrobial peptides and compositions
US7674771B2 (en) *	2003-10-29	2010-03-09	Toagosei Co., Ltd	Antimicrobial peptides and utilization of the same
US20050209563A1 (en) *	2004-03-19	2005-09-22	Peter Hopping	Cassette-based dialysis medical fluid therapy systems, apparatuses and methods
JP4507080B2 (ja) *	2004-07-30	2010-07-21	東亞合成株式会社	抗菌ペプチド及びその利用
JP4730584B2 (ja) *	2004-12-06	2011-07-20	東亞合成株式会社	抗菌ペプチド及びその利用
US8252737B2 (en)	2004-12-15	2012-08-28	The Regents Of The University Of Colorado	Antimicrobial peptides and methods of use
EP1849474B1 (en) *	2005-02-15	2016-09-07	Toagosei Co., Ltd.	Antimicrobial peptide and use thereof
US7731689B2 (en)	2007-02-15	2010-06-08	Baxter International Inc.	Dialysis system having inductive heating
US8558964B2 (en)	2007-02-15	2013-10-15	Baxter International Inc.	Dialysis system having display with electromagnetic compliance (“EMC”) seal
US8361023B2 (en) *	2007-02-15	2013-01-29	Baxter International Inc.	Dialysis system with efficient battery back-up
US8870812B2 (en) *	2007-02-15	2014-10-28	Baxter International Inc.	Dialysis system having video display with ambient light adjustment
US7998115B2 (en) *	2007-02-15	2011-08-16	Baxter International Inc.	Dialysis system having optical flowrate detection
DK2178549T3 (en) *	2007-07-26	2017-01-09	Revance Therapeutics Inc	Antimicrobial peptide AND COMPOSITIONS THEREOF
WO2010042534A1 (en) *	2008-10-06	2010-04-15	The Regents Of The University Of Colorado, A Body Corporate	Peptides and methods of use
GB0821616D0 (en) *	2008-11-26	2008-12-31	Lytix Biopharma As	Compounds
EP2437770A4 (en) *	2009-06-05	2013-11-06	Univ Colorado Regents	ANTIMICROBIAL PEPTIDES
WO2011068801A2 (en)	2009-12-01	2011-06-09	The Rockefeller University	Methods for identifying compounds that modulate ion channel activity of a kir channel
SI2558577T1 (sl)	2010-04-16	2019-05-31	Nuevolution A/S	Bifunkcionalni kompleksi in metode za pripravo in uporabo takšnih kompleksov
EP3384938A1 (en)	2011-09-12	2018-10-10	Moderna Therapeutics, Inc.	Engineered nucleic acids and methods of use thereof
WO2013151664A1 (en)	2012-04-02	2013-10-10	modeRNA Therapeutics	Modified polynucleotides for the production of proteins
CN104411338A (zh)	2012-04-02	2015-03-11	现代治疗公司	用于产生与人类疾病相关的生物制剂和蛋白质的修饰多核苷酸
US20150072922A1 (en) *	2012-04-17	2015-03-12	The Research Institute At Nationwide Children's Hospital	Rnase 7 antimicrobial peptides
MY151307A (en) *	2012-06-18	2014-05-05	Univ Malaya	Peptides having antimicrobial activity
GB201401877D0 (en)	2014-02-04	2014-03-19	Univ Tromsoe	Peptides
EP3067608A1 (en) *	2015-03-10	2016-09-14	Abu Dhabi Polymers Co. Ltd (Borouge) LLC.	Eccentric polyolefin pipe
US11168131B2 (en)	2015-11-10	2021-11-09	Visterra, Inc.	Antibody molecule-drug conjugates and uses thereof
WO2018136626A1 (en)	2017-01-18	2018-07-26	Visterra, Inc.	Antibody molecule-drug conjugates and uses thereof
US11021529B2 (en)	2017-03-03	2021-06-01	Massachusetts Institute Of Technology	Antimicrobial constructs and uses thereof
US10934943B2 (en)	2017-04-27	2021-03-02	General Electric Company	Compressor apparatus with bleed slot and supplemental flange
US11179516B2 (en)	2017-06-22	2021-11-23	Baxter International Inc.	Systems and methods for incorporating patient pressure into medical fluid delivery
KR20240085798A (ko)	2020-04-03	2024-06-17	비스테라, 인크.	항체 분자-약물 접합체 및 이의 용도
CU24750B1 (es) *	2020-11-19	2025-06-11	Centro De Investig Y Desarrollo De Medicamentos Cidem	Entidades peptídicas con actividad antimicrobiana frente a patógenos multi-drogoresistentes

Family Cites Families (35)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5206154A (en)	1985-01-28	1993-04-27	Xoma Corporation	Method of producing cecropins by microbiological techniques
US5028530A (en)	1985-01-28	1991-07-02	Xoma Corporation	AraB promoters and method of producing polypeptides, including cecropins, by microbiological techniques
US5166321A (en)	1985-01-28	1992-11-24	International Genetic Engineering, Inc.	Cecropin polypetides with activity against Gram-positive and Gram-negative bacteria
US4810777A (en)	1987-03-04	1989-03-07	The United States Of America As Represented By The Department Of Health And Human Services	Antimicrobial compounds
US4822608A (en)	1987-09-14	1989-04-18	Vespa Laboratories, Inc.	Methods and compositions for the treatment of mammalian infections employing medicaments comprising hymenoptera venom or proteinaceous or polypeptide components thereof
EP0416035B1 (en)	1988-05-27	1994-12-07	The Children's Hospital Of Philadelphia	Amphiphilic peptides and use thereof
SE8802939D0 (sv)	1988-08-19	1988-08-19	Kabigen Ab	A method for the production and isolation of a fusion protein in eukaryotic cells
HUT57992A (en)	1988-10-21	1992-01-28	Magainin Sciences Inc	Process for producing composition comprising biologically active peptides and certain anions
EP0440688B1 (en)	1988-10-21	1994-09-21	The Children's Hospital Of Philadelphia	Cpf peptide compositions and uses
US5217956A (en)	1988-10-21	1993-06-08	The Children's Hospital Of Philadelphia	Composition and treatment with biologically active peptides and certain anions
CA2007913A1 (en)	1989-01-30	1990-07-30	Michael Zasloff	Composition and treatment with peptide combinations
US5254535A (en)	1989-04-17	1993-10-19	The Children's Hospital Of Pennsylvania	Composition and treatment with biologically active peptides and antibiotic
FR2646777B1 (fr)	1989-05-12	1993-09-03	Bio Serae Lab	Procede de preparation d'un produit particulaire antimicrobien, produit antimicrobien obtenu et applications
US5073542A (en)	1989-06-07	1991-12-17	Magainin Sciences Inc.	CPF peptide compositions and their use in inhibiting growth of target cells or a virus
US5045531A (en)	1989-12-18	1991-09-03	Magainin Sciences Inc.	Wound treatment employing biologically active ion channel forming peptides and proteins
JPH07504152A (ja)	1990-02-08	1995-05-11	マゲイニン　ファーマスーティカルズ，　インコーポレーテッド	生物活性ペプチドおよび標的細胞、ウイルス、あるいはウイルス感染細胞の成長を抑制する方法
US5227469A (en)	1990-02-14	1993-07-13	Genentech, Inc.	Platelet aggregation inhibitors from the leech
JPH05509295A (ja)	1990-04-23	1993-12-22	マゲイニン　サイエンセズ　インコーポレーテッド	生物学的に活性なペプチドおよび毒性陽イオンを有する組成物およびこれらを使用する治療法
JPH05507077A (ja)	1990-04-27	1993-10-14	マゲイニン　サイエンセズ　インコーポレーテッド	生物活性ペプチドおよび駆虫剤もしくは抗真菌剤を使う組成物および治療法
JPH05507273A (ja)	1990-05-14	1993-10-21	マゲイニン　サイエンセズ　インコーポレーテッド	Ｄアミノ酸残基を有する生物活性ペプチドの組成物およびそれによる治療方法
US5208220A (en)	1990-06-27	1993-05-04	Magainin Pharmaceuticals, Inc.	Composition and treatment with biologically active peptides and antibiotics which inhibit DNA gyrase
US5202420A (en)	1990-10-25	1993-04-13	The Children's Hospital Of Philadelphia	Tracheal antimicrobial peptides, dna sequences and methods for the production and use thereof
US5235038A (en)	1991-01-22	1993-08-10	Torry Pines Institute For Molecular Studies	Deletion and substitution analogues of melittin peptide
CA2107674A1 (en)	1991-04-08	1992-10-09	W. Lee Maloy	Novel peptide compositions and uses therefor
JPH06511234A (ja)	1991-06-12	1994-12-15	マゲイニン　ファーマス−ティカルズ，インコーポレーテッド	Ｃ末端置換を有する生物活性ペプチド組成物および治療法
WO1993001723A1 (en)	1991-07-25	1993-02-04	Magainin Pharmaceuticals, Inc.	Prophylaxis and treatment of adverse oral conditions with biologically active peptides
US5547939A (en) *	1991-06-14	1996-08-20	The Regents Of The University Of California	Broad spectrum antimicrobial compounds and methods of use
US5324716A (en) *	1991-06-14	1994-06-28	Regents Of The University Of California	Broad spectrum antimicrobial compounds and methods of use
JPH07501519A (ja)	1991-09-13	1995-02-16	マゲイニン　ファーマスーティカルズ，インコーポレーテッド	生物活性両親媒性ペプチド組成物およびその用途
WO1993011783A1 (en)	1991-12-09	1993-06-24	Magainin Pharmaceuticals Inc.	Composition and treatment with biologically active peptides and chelating agents
CA2137087A1 (en)	1992-06-01	1993-12-09	U. Prasad Kari	Biologically active peptides having n-terminal substitutions
WO1994004688A2 (en) *	1992-08-21	1994-03-03	The University Of British Columbia	Cationic peptides and method for production
CA2106720C (en)	1992-09-23	1997-12-16	Charles L. Deschenes	Needle for use as part of a plastic fastener dispensing tool
US5635594A (en) *	1994-03-11	1997-06-03	University Of California, Los Angeles	Gallinacins - antibiotic peptides
US5877274A (en)	1995-06-02	1999-03-02	University Of British Columbia	Antimicrobial cationic peptides

1996
- 1996-08-23 DE DE69637731T patent/DE69637731D1/de not_active Expired - Lifetime
- 1996-08-23 WO PCT/IB1996/000996 patent/WO1997008199A2/en not_active Ceased
- 1996-08-23 AU AU69407/96A patent/AU6940796A/en not_active Abandoned
- 1996-08-23 US US08/702,054 patent/US6191254B1/en not_active Expired - Fee Related
- 1996-08-23 JP JP51006897A patent/JP3860838B2/ja not_active Expired - Fee Related
- 1996-08-23 CA CA002230160A patent/CA2230160A1/en not_active Abandoned
- 1996-08-23 EP EP96930303A patent/EP0846128B1/en not_active Expired - Lifetime
- 1996-08-23 AT AT96930303T patent/ATE412668T1/de not_active IP Right Cessation
- 1996-08-23 ES ES96930303T patent/ES2316154T3/es not_active Expired - Lifetime
2003
- 2003-03-28 US US10/403,104 patent/US7390873B2/en not_active Expired - Fee Related

Also Published As

Publication number	Publication date
JP3860838B2 (ja)	2006-12-20
DE69637731D1 (de)	2008-12-11
CA2230160A1 (en)	1997-03-06
ATE412668T1 (de)	2008-11-15
EP0846128A2 (en)	1998-06-10
US20040019181A1 (en)	2004-01-29
WO1997008199A3 (en)	1997-09-12
EP0846128B1 (en)	2008-10-29
HK1011867A1 (en)	1999-07-23
AU6940796A (en)	1997-03-19
US6191254B1 (en)	2001-02-20
WO1997008199A2 (en)	1997-03-06
JPH11511971A (ja)	1999-10-19
US7390873B2 (en)	2008-06-24

Publication	Publication Date	Title
US7390873B2 (en)	2008-06-24	Antimicrobial cationic peptides
US6465429B1 (en)	2002-10-15	Antimicrobial cationic peptides
DK2938352T3 (en)	2018-08-20	CYLIC CATIONIC PEPTIDES WITH ANTIBMICROBIAL ACTIVITY
Jung et al.	2007	Fungicidal effect of pleurocidin by membrane-active mechanism and design of enantiomeric analogue for proteolytic resistance
US6040435A (en)	2000-03-21	Antimicrobial cationic peptides
US20110262508A1 (en)	2011-10-27	Antimicrobial compositions, formulations and uses thereof
JPH08508165A (ja)	1996-09-03	ウシ好中球由来の新規な抗微生物性ペプチド
JP2001503020A (ja)	2001-03-06	広域抗菌活性を有する環状ペプチド
JP2001520631A (ja)	2001-10-30	抗真菌性ペプチド
Wood et al.	2014	Modified cysteine-deleted tachyplesin (CDT) analogs as linear antimicrobial peptides: Influence of chain length, positive charge, and hydrophobicity on antimicrobial and hemolytic activity
JPH09509175A (ja)	1997-09-16	広域スペクトル抗菌化合物と使用方法
US20080234188A1 (en)	2008-09-25	Antimicrobial Peptides
EP0824547B1 (en)	2003-12-10	Anti-fungal peptides
JPH08500818A (ja)	1996-01-30	Ｎ末端置換を有する生物活性ペプチド
EP1294745A2 (en)	2003-03-26	Antimicrobial peptides and methods of use thereof
JP4902919B2 (ja)	2012-03-21	ペプチド作成の方法
Shafer et al.	2002	Tailoring an antibacterial peptide of human lysosomal cathepsin G to enhance its broad-spectrum action against antibiotic-resistant bacterial pathogens
US5654274A (en)	1997-08-05	Biologically active peptides having N-terminal substitutions
WO1999060016A2 (en)	1999-11-25	Antimicrobial cationic peptide derivatives of bactenecin
AU2002317071A1 (en)	2003-06-19	Antimicrobial peptides
WO2016184855A1 (en)	2016-11-24	New amino acid sequences with microbicidal activity derived from naja atra cardiotoxin 1 (ctx-1)
JPH09507669A (ja)	1997-08-05	Ｎ末端修飾を有する両親媒性のイオンチャンネル形成ペプチド
CN112778424B (zh)	2022-07-26	嵌合肽r7及其应用
TW202317598A (zh)	2023-05-01	具有抗微生物活性的胜肽
JP2001510164A (ja)	2001-07-31	動物に対する毒性を減じた生物活性ペプチドおよび同ペプチドを調製する方法。