ZA200609401B - Sustained release formulations - Google Patents

Sustained release formulations Download PDF

Info

Publication number: ZA200609401B
Authority: ZA; South Africa
Prior art keywords: peptide; acid ester; gallic acid; complex; salt
Prior art date: 2004-04-23

Application number

ZA200609401A

Other languages

English (en)

Inventor

Merrill S Goldenberg

Gu Jian Hua

Original Assignee

Amgen Inc

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.)

2004-04-23

Filing date

2006-11-13

Publication date

2008-05-28

2006-11-13 Application filed by Amgen Inc filed Critical Amgen Inc

2008-05-28 Publication of ZA200609401B publication Critical patent/ZA200609401B/en

Links

239000000203 mixture Substances 0.000 title claims description 53
238000013268 sustained release Methods 0.000 title claims description 31
239000012730 sustained-release form Substances 0.000 title claims description 31
238000009472 formulation Methods 0.000 title claims description 24
108090000765 processed proteins & peptides Proteins 0.000 claims description 106
QJYNZEYHSMRWBK-NIKIMHBISA-N 1,2,3,4,6-pentakis-O-galloyl-beta-D-glucose Chemical group OC1=C(O)C(O)=CC(C(=O)OC[C@@H]2[C@H]([C@H](OC(=O)C=3C=C(O)C(O)=C(O)C=3)[C@@H](OC(=O)C=3C=C(O)C(O)=C(O)C=3)[C@H](OC(=O)C=3C=C(O)C(O)=C(O)C=3)O2)OC(=O)C=2C=C(O)C(O)=C(O)C=2)=C1 QJYNZEYHSMRWBK-NIKIMHBISA-N 0.000 claims description 86
LNTHITQWFMADLM-UHFFFAOYSA-N anhydrous gallic acid Natural products OC(=O)C1=CC(O)=C(O)C(O)=C1 LNTHITQWFMADLM-UHFFFAOYSA-N 0.000 claims description 68
-1 gallic acid ester Chemical class 0.000 claims description 63
102000004169 proteins and genes Human genes 0.000 claims description 63
108090000623 proteins and genes Proteins 0.000 claims description 63
235000004515 gallic acid Nutrition 0.000 claims description 59
229940074391 gallic acid Drugs 0.000 claims description 59
150000003839 salts Chemical group 0.000 claims description 35
WMBWREPUVVBILR-WIYYLYMNSA-N (-)-Epigallocatechin-3-o-gallate Chemical compound O([C@@H]1CC2=C(O)C=C(C=C2O[C@@H]1C=1C=C(O)C(O)=C(O)C=1)O)C(=O)C1=CC(O)=C(O)C(O)=C1 WMBWREPUVVBILR-WIYYLYMNSA-N 0.000 claims description 24
WMBWREPUVVBILR-UHFFFAOYSA-N GCG Natural products C=1C(O)=C(O)C(O)=CC=1C1OC2=CC(O)=CC(O)=C2CC1OC(=O)C1=CC(O)=C(O)C(O)=C1 WMBWREPUVVBILR-UHFFFAOYSA-N 0.000 claims description 24
229940030275 epigallocatechin gallate Drugs 0.000 claims description 24
238000000034 method Methods 0.000 claims description 22
239000002244 precipitate Substances 0.000 claims description 18
239000008194 pharmaceutical composition Substances 0.000 claims description 15
150000001413 amino acids Chemical class 0.000 claims description 12
108010050297 hydroxyprolyl-glycine Proteins 0.000 claims description 10
241001465754 Metazoa Species 0.000 claims description 8
238000004519 manufacturing process Methods 0.000 claims description 8
108060003951 Immunoglobulin Proteins 0.000 claims description 7
102000018358 immunoglobulin Human genes 0.000 claims description 7
WFDSWNXTPKLLOT-UHNVWZDZSA-N 2-[[(2s,4r)-4-hydroxypyrrolidin-1-ium-2-carbonyl]amino]acetate Chemical compound O[C@H]1CN[C@H](C(=O)NCC(O)=O)C1 WFDSWNXTPKLLOT-UHNVWZDZSA-N 0.000 claims description 5
FUKDBQGFSJUXGX-RWMBFGLXSA-N Lys-Arg-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CCCCN)N)C(=O)O FUKDBQGFSJUXGX-RWMBFGLXSA-N 0.000 claims description 5
ONPXCLZMBSJLSP-CSMHCCOUSA-N Pro-Hyp Chemical compound C1[C@H](O)C[C@@H](C(O)=O)N1C(=O)[C@H]1NCCC1 ONPXCLZMBSJLSP-CSMHCCOUSA-N 0.000 claims description 5
ZJWIXBZTAAJERF-IHRRRGAJSA-N Lys-Lys-Arg Chemical compound NCCCC[C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(O)=O)CCCN=C(N)N ZJWIXBZTAAJERF-IHRRRGAJSA-N 0.000 claims description 4
125000000218 acetic acid group Chemical group C(C)(=O)* 0.000 claims description 4
239000005557 antagonist Substances 0.000 claims description 4
108010060035 arginylproline Proteins 0.000 claims description 4
239000003937 drug carrier Substances 0.000 claims description 3
239000012634 fragment Substances 0.000 claims description 3
238000002156 mixing Methods 0.000 claims description 3
239000000546 pharmaceutical excipient Substances 0.000 claims description 3
PMMYEEVYMWASQN-DMTCNVIQSA-N Hydroxyproline Chemical compound O[C@H]1CN[C@H](C(O)=O)C1 PMMYEEVYMWASQN-DMTCNVIQSA-N 0.000 claims 4
BWKMGYQJPOAASG-UHFFFAOYSA-N 1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid Chemical compound C1=CC=C2CNC(C(=O)O)CC2=C1 BWKMGYQJPOAASG-UHFFFAOYSA-N 0.000 claims 2
LRHRHAWNXCGABU-UHFFFAOYSA-N 2-(cyclopentylazaniumyl)acetate Chemical compound OC(=O)CNC1CCCC1 LRHRHAWNXCGABU-UHFFFAOYSA-N 0.000 claims 2
AHLPHDHHMVZTML-BYPYZUCNSA-N L-Ornithine Chemical compound NCCC[C@H](N)C(O)=O AHLPHDHHMVZTML-BYPYZUCNSA-N 0.000 claims 2
AHLPHDHHMVZTML-UHFFFAOYSA-N Orn-delta-NH2 Natural products NCCCC(N)C(O)=O AHLPHDHHMVZTML-UHFFFAOYSA-N 0.000 claims 2
UTJLXEIPEHZYQJ-UHFFFAOYSA-N Ornithine Natural products OC(=O)C(C)CCCN UTJLXEIPEHZYQJ-UHFFFAOYSA-N 0.000 claims 2
229940083963 Peptide antagonist Drugs 0.000 claims 2
PMMYEEVYMWASQN-UHFFFAOYSA-N dl-hydroxyproline Natural products OC1C[NH2+]C(C([O-])=O)C1 PMMYEEVYMWASQN-UHFFFAOYSA-N 0.000 claims 2
229960003104 ornithine Drugs 0.000 claims 2
PMMYEEVYMWASQN-IMJSIDKUSA-N trans-4-Hydroxy-L-proline Natural products O[C@@H]1CN[C@H](C(O)=O)C1 PMMYEEVYMWASQN-IMJSIDKUSA-N 0.000 claims 2
230000002459 sustained effect Effects 0.000 description 17
HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 15
101800005149 Peptide B Proteins 0.000 description 14
239000013543 active substance Substances 0.000 description 12
239000000243 solution Substances 0.000 description 12
102000004196 processed proteins & peptides Human genes 0.000 description 10
102000005962 receptors Human genes 0.000 description 10
108020003175 receptors Proteins 0.000 description 10
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 10
102000037865 fusion proteins Human genes 0.000 description 9
108020001507 fusion proteins Proteins 0.000 description 9
230000015572 biosynthetic process Effects 0.000 description 8
239000003446 ligand Substances 0.000 description 8
229920002253 Tannate Polymers 0.000 description 7
238000001727 in vivo Methods 0.000 description 7
229920000642 polymer Polymers 0.000 description 7
239000003795 chemical substances by application Substances 0.000 description 6
239000003814 drug Substances 0.000 description 6
238000012377 drug delivery Methods 0.000 description 6
239000000463 material Substances 0.000 description 6
239000000843 powder Substances 0.000 description 6
102000004127 Cytokines Human genes 0.000 description 5
108090000695 Cytokines Proteins 0.000 description 5
108060008683 Tumor Necrosis Factor Receptor Proteins 0.000 description 5
102100040247 Tumor necrosis factor Human genes 0.000 description 5
229940079593 drug Drugs 0.000 description 5
239000011859 microparticle Substances 0.000 description 5
238000002360 preparation method Methods 0.000 description 5
102000003298 tumor necrosis factor receptor Human genes 0.000 description 5
238000005119 centrifugation Methods 0.000 description 4
238000002347 injection Methods 0.000 description 4
239000007924 injection Substances 0.000 description 4
239000006194 liquid suspension Substances 0.000 description 4
239000007787 solid Substances 0.000 description 4
239000007962 solid dispersion Substances 0.000 description 4
239000002904 solvent Substances 0.000 description 4
239000011550 stock solution Substances 0.000 description 4
101800004538 Bradykinin Proteins 0.000 description 3
108010029697 CD40 Ligand Proteins 0.000 description 3
102100032937 CD40 ligand Human genes 0.000 description 3
LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 3
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
101000611183 Homo sapiens Tumor necrosis factor Proteins 0.000 description 3
108010002386 Interleukin-3 Proteins 0.000 description 3
102100039064 Interleukin-3 Human genes 0.000 description 3
108010038036 Receptor Activator of Nuclear Factor-kappa B Proteins 0.000 description 3
102000010498 Receptor Activator of Nuclear Factor-kappa B Human genes 0.000 description 3
102100024598 Tumor necrosis factor ligand superfamily member 10 Human genes 0.000 description 3
101710097160 Tumor necrosis factor ligand superfamily member 10 Proteins 0.000 description 3
230000000694 effects Effects 0.000 description 3
238000001914 filtration Methods 0.000 description 3
108010091748 peptide A Proteins 0.000 description 3
229920001606 poly(lactic acid-co-glycolic acid) Polymers 0.000 description 3
239000006228 supernatant Substances 0.000 description 3
102000055006 Calcitonin Human genes 0.000 description 2
108060001064 Calcitonin Proteins 0.000 description 2
239000000055 Corticotropin-Releasing Hormone Substances 0.000 description 2
108020004414 DNA Proteins 0.000 description 2
108010032976 Enfuvirtide Proteins 0.000 description 2
102000004190 Enzymes Human genes 0.000 description 2
108090000790 Enzymes Proteins 0.000 description 2
108010008165 Etanercept Proteins 0.000 description 2
108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 description 2
102100039620 Granulocyte-macrophage colony-stimulating factor Human genes 0.000 description 2
108010051696 Growth Hormone Proteins 0.000 description 2
108090000581 Leukemia inhibitory factor Proteins 0.000 description 2
102000004058 Leukemia inhibitory factor Human genes 0.000 description 2
206010028980 Neoplasm Diseases 0.000 description 2
108010025020 Nerve Growth Factor Proteins 0.000 description 2
108090000630 Oncostatin M Proteins 0.000 description 2
102000004140 Oncostatin M Human genes 0.000 description 2
108090000445 Parathyroid hormone Proteins 0.000 description 2
102000001253 Protein Kinase Human genes 0.000 description 2
241000700159 Rattus Species 0.000 description 2
102000005157 Somatostatin Human genes 0.000 description 2
108010056088 Somatostatin Proteins 0.000 description 2
102100038803 Somatotropin Human genes 0.000 description 2
239000007983 Tris buffer Substances 0.000 description 2
108060008682 Tumor Necrosis Factor Proteins 0.000 description 2
159000000021 acetate salts Chemical class 0.000 description 2
125000000539 amino acid group Chemical group 0.000 description 2
239000000427 antigen Substances 0.000 description 2
102000036639 antigens Human genes 0.000 description 2
108091007433 antigens Proteins 0.000 description 2
238000013459 approach Methods 0.000 description 2
239000007864 aqueous solution Substances 0.000 description 2
230000008901 benefit Effects 0.000 description 2
230000027455 binding Effects 0.000 description 2
229920000249 biocompatible polymer Polymers 0.000 description 2
229920002988 biodegradable polymer Polymers 0.000 description 2
239000004621 biodegradable polymer Substances 0.000 description 2
238000006065 biodegradation reaction Methods 0.000 description 2
230000004071 biological effect Effects 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
229960004015 calcitonin Drugs 0.000 description 2
210000004027 cell Anatomy 0.000 description 2
150000001875 compounds Chemical class 0.000 description 2
230000001419 dependent effect Effects 0.000 description 2
PEASPLKKXBYDKL-FXEVSJAOSA-N enfuvirtide Chemical compound C([C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)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(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(C)=O)[C@@H](C)O)[C@@H](C)CC)C1=CN=CN1 PEASPLKKXBYDKL-FXEVSJAOSA-N 0.000 description 2
229960000403 etanercept Drugs 0.000 description 2
239000003102 growth factor Substances 0.000 description 2
239000000122 growth hormone Substances 0.000 description 2
229940088597 hormone Drugs 0.000 description 2
239000005556 hormone Substances 0.000 description 2
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 2
229920000747 poly(lactic acid) Polymers 0.000 description 2
229940065514 poly(lactide) Drugs 0.000 description 2
239000000047 product Substances 0.000 description 2
108060006633 protein kinase Proteins 0.000 description 2
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 2
229960000553 somatostatin Drugs 0.000 description 2
238000003756 stirring Methods 0.000 description 2
238000007920 subcutaneous administration Methods 0.000 description 2
239000000126 substance Substances 0.000 description 2
LRBQNJMCXXYXIU-NRMVVENXSA-N tannic acid Chemical compound OC1=C(O)C(O)=CC(C(=O)OC=2C(=C(O)C=C(C=2)C(=O)OC[C@@H]2[C@H]([C@H](OC(=O)C=3C=C(OC(=O)C=4C=C(O)C(O)=C(O)C=4)C(O)=C(O)C=3)[C@@H](OC(=O)C=3C=C(OC(=O)C=4C=C(O)C(O)=C(O)C=4)C(O)=C(O)C=3)[C@@H](OC(=O)C=3C=C(OC(=O)C=4C=C(O)C(O)=C(O)C=4)C(O)=C(O)C=3)O2)OC(=O)C=2C=C(OC(=O)C=3C=C(O)C(O)=C(O)C=3)C(O)=C(O)C=2)O)=C1 LRBQNJMCXXYXIU-NRMVVENXSA-N 0.000 description 2
235000015523 tannic acid Nutrition 0.000 description 2
229920002258 tannic acid Polymers 0.000 description 2
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
RWBLWXCGQLZKLK-USVTTYPOSA-N (2s)-2-[(2-aminoacetyl)amino]-n-[(2s)-1-[[(2s)-1-[[(2s)-1-[[(2s)-1-[[2-[[(2s)-1-[[(2s)-1-[[(2s)-1-amino-4-methylsulfanyl-1-oxobutan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-3-(1h-imidazol-5-yl)-1-oxopropan-2-yl]amino]-2-oxoethyl]amino]-3-methyl-1-oxob Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(N)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CC(N)=O)NC(=O)CN)C(C)C)C1=CN=CN1 RWBLWXCGQLZKLK-USVTTYPOSA-N 0.000 description 1
MZOFCQQQCNRIBI-VMXHOPILSA-N (3s)-4-[[(2s)-1-[[(2s)-1-[[(1s)-1-carboxy-2-hydroxyethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-3-[[2-[[(2s)-2,6-diaminohexanoyl]amino]acetyl]amino]-4-oxobutanoic acid Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN MZOFCQQQCNRIBI-VMXHOPILSA-N 0.000 description 1
TUSDEZXZIZRFGC-UHFFFAOYSA-N 1-O-galloyl-3,6-(R)-HHDP-beta-D-glucose Natural products OC1C(O2)COC(=O)C3=CC(O)=C(O)C(O)=C3C3=C(O)C(O)=C(O)C=C3C(=O)OC1C(O)C2OC(=O)C1=CC(O)=C(O)C(O)=C1 TUSDEZXZIZRFGC-UHFFFAOYSA-N 0.000 description 1
108091007505 ADAM17 Proteins 0.000 description 1
QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
102100026277 Alpha-galactosidase A Human genes 0.000 description 1
102000004881 Angiotensinogen Human genes 0.000 description 1
108090001067 Angiotensinogen Proteins 0.000 description 1
108010064733 Angiotensins Proteins 0.000 description 1
102000015427 Angiotensins Human genes 0.000 description 1
102000005666 Apolipoprotein A-I Human genes 0.000 description 1
108010059886 Apolipoprotein A-I Proteins 0.000 description 1
102100029470 Apolipoprotein E Human genes 0.000 description 1
101710095339 Apolipoprotein E Proteins 0.000 description 1
102100022005 B-lymphocyte antigen CD20 Human genes 0.000 description 1
108010051479 Bombesin Proteins 0.000 description 1
102000013585 Bombesin Human genes 0.000 description 1
102400000967 Bradykinin Human genes 0.000 description 1
102400000667 Brain natriuretic peptide 32 Human genes 0.000 description 1
101800000407 Brain natriuretic peptide 32 Proteins 0.000 description 1
101800002247 Brain natriuretic peptide 45 Proteins 0.000 description 1
102100032528 C-type lectin domain family 11 member A Human genes 0.000 description 1
101710167766 C-type lectin domain family 11 member A Proteins 0.000 description 1
108010046080 CD27 Ligand Proteins 0.000 description 1
102100027207 CD27 antigen Human genes 0.000 description 1
108010017987 CD30 Ligand Proteins 0.000 description 1
101150013553 CD40 gene Proteins 0.000 description 1
102100025221 CD70 antigen Human genes 0.000 description 1
OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical group [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
108050004290 Cecropin Proteins 0.000 description 1
108010055166 Chemokine CCL5 Proteins 0.000 description 1
102000001327 Chemokine CCL5 Human genes 0.000 description 1
102100025841 Cholecystokinin Human genes 0.000 description 1
101800001982 Cholecystokinin Proteins 0.000 description 1
102100022641 Coagulation factor IX Human genes 0.000 description 1
102000007644 Colony-Stimulating Factors Human genes 0.000 description 1
108010071942 Colony-Stimulating Factors Proteins 0.000 description 1
102400000739 Corticotropin Human genes 0.000 description 1
101800000414 Corticotropin Proteins 0.000 description 1
108010022152 Corticotropin-Releasing Hormone Proteins 0.000 description 1
102000012289 Corticotropin-Releasing Hormone Human genes 0.000 description 1
241000701022 Cytomegalovirus Species 0.000 description 1
108050001718 Death domains Proteins 0.000 description 1
102000010170 Death domains Human genes 0.000 description 1
102100031111 Disintegrin and metalloproteinase domain-containing protein 17 Human genes 0.000 description 1
102400000242 Dynorphin A(1-17) Human genes 0.000 description 1
108010065372 Dynorphins Proteins 0.000 description 1
102100029722 Ectonucleoside triphosphate diphosphohydrolase 1 Human genes 0.000 description 1
108010092674 Enkephalins Proteins 0.000 description 1
102400001368 Epidermal growth factor Human genes 0.000 description 1
101800003838 Epidermal growth factor Proteins 0.000 description 1
102000003951 Erythropoietin Human genes 0.000 description 1
108090000394 Erythropoietin Proteins 0.000 description 1
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
239000001263 FEMA 3042 Substances 0.000 description 1
108010076282 Factor IX Proteins 0.000 description 1
108010054218 Factor VIII Proteins 0.000 description 1
102000001690 Factor VIII Human genes 0.000 description 1
102100020715 Fms-related tyrosine kinase 3 ligand protein Human genes 0.000 description 1
101710162577 Fms-related tyrosine kinase 3 ligand protein Proteins 0.000 description 1
108700012941 GNRH1 Proteins 0.000 description 1
102400001370 Galanin Human genes 0.000 description 1
101800002068 Galanin Proteins 0.000 description 1
102400000921 Gastrin Human genes 0.000 description 1
102000004862 Gastrin releasing peptide Human genes 0.000 description 1
108090001053 Gastrin releasing peptide Proteins 0.000 description 1
108010052343 Gastrins Proteins 0.000 description 1
102400000321 Glucagon Human genes 0.000 description 1
108060003199 Glucagon Proteins 0.000 description 1
108010088406 Glucagon-Like Peptides Proteins 0.000 description 1
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 1
108010017544 Glucosylceramidase Proteins 0.000 description 1
102000004547 Glucosylceramidase Human genes 0.000 description 1
239000000579 Gonadotropin-Releasing Hormone Substances 0.000 description 1
108010017080 Granulocyte Colony-Stimulating Factor Proteins 0.000 description 1
102000004269 Granulocyte Colony-Stimulating Factor Human genes 0.000 description 1
108010054017 Granulocyte Colony-Stimulating Factor Receptors Proteins 0.000 description 1
102100039622 Granulocyte colony-stimulating factor receptor Human genes 0.000 description 1
108010092372 Granulocyte-Macrophage Colony-Stimulating Factor Receptors Proteins 0.000 description 1
102000016355 Granulocyte-Macrophage Colony-Stimulating Factor Receptors Human genes 0.000 description 1
QXZGBUJJYSLZLT-UHFFFAOYSA-N H-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-OH Natural products NC(N)=NCCCC(N)C(=O)N1CCCC1C(=O)N1C(C(=O)NCC(=O)NC(CC=2C=CC=CC=2)C(=O)NC(CO)C(=O)N2C(CCC2)C(=O)NC(CC=2C=CC=CC=2)C(=O)NC(CCCN=C(N)N)C(O)=O)CCC1 QXZGBUJJYSLZLT-UHFFFAOYSA-N 0.000 description 1
241000282412 Homo Species 0.000 description 1
101000897405 Homo sapiens B-lymphocyte antigen CD20 Proteins 0.000 description 1
101000914511 Homo sapiens CD27 antigen Proteins 0.000 description 1
101001012447 Homo sapiens Ectonucleoside triphosphate diphosphohydrolase 1 Proteins 0.000 description 1
101000935040 Homo sapiens Integrin beta-2 Proteins 0.000 description 1
101000738771 Homo sapiens Receptor-type tyrosine-protein phosphatase C Proteins 0.000 description 1
101000851376 Homo sapiens Tumor necrosis factor receptor superfamily member 8 Proteins 0.000 description 1
108700022013 Insecta cecropin B Proteins 0.000 description 1
102000004877 Insulin Human genes 0.000 description 1
108090001061 Insulin Proteins 0.000 description 1
108090000723 Insulin-Like Growth Factor I Proteins 0.000 description 1
102100025390 Integrin beta-2 Human genes 0.000 description 1
108050006617 Interleukin-1 receptor Proteins 0.000 description 1
102000019223 Interleukin-1 receptor Human genes 0.000 description 1
102000004556 Interleukin-15 Receptors Human genes 0.000 description 1
108010017535 Interleukin-15 Receptors Proteins 0.000 description 1
102000004554 Interleukin-17 Receptors Human genes 0.000 description 1
108010017525 Interleukin-17 Receptors Proteins 0.000 description 1
102000004557 Interleukin-18 Receptors Human genes 0.000 description 1
108010017537 Interleukin-18 Receptors Proteins 0.000 description 1
108010002350 Interleukin-2 Proteins 0.000 description 1
102000010787 Interleukin-4 Receptors Human genes 0.000 description 1
108010038486 Interleukin-4 Receptors Proteins 0.000 description 1
102000015696 Interleukins Human genes 0.000 description 1
108010063738 Interleukins Proteins 0.000 description 1
102000036770 Islet Amyloid Polypeptide Human genes 0.000 description 1
108010041872 Islet Amyloid Polypeptide Proteins 0.000 description 1
108010003195 Kallidin Proteins 0.000 description 1
FYSKZKQBTVLYEQ-FSLKYBNLSA-N Kallidin Chemical compound NCCCC[C@H](N)C(=O)N[C@@H](CCCN=C(N)N)C(=O)N1CCC[C@H]1C(=O)N1[C@H](C(=O)NCC(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CO)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CCCN=C(N)N)C(O)=O)CCC1 FYSKZKQBTVLYEQ-FSLKYBNLSA-N 0.000 description 1
102100020880 Kit ligand Human genes 0.000 description 1
101710177504 Kit ligand Proteins 0.000 description 1
URLZCHNOLZSCCA-VABKMULXSA-N Leu-enkephalin Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(O)=O)NC(=O)CNC(=O)CNC(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=CC=C1 URLZCHNOLZSCCA-VABKMULXSA-N 0.000 description 1
NPBGTPKLVJEOBE-IUCAKERBSA-N Lys-Arg Chemical compound NCCCC[C@H](N)C(=O)N[C@H](C(O)=O)CCCNC(N)=N NPBGTPKLVJEOBE-IUCAKERBSA-N 0.000 description 1
101800004760 Magainin-1 Proteins 0.000 description 1
241000124008 Mammalia Species 0.000 description 1
102400001132 Melanin-concentrating hormone Human genes 0.000 description 1
101800002739 Melanin-concentrating hormone Proteins 0.000 description 1
101710151321 Melanostatin Proteins 0.000 description 1
241001529936 Murinae Species 0.000 description 1
101000845218 Mus musculus Thymic stromal lymphopoietin Proteins 0.000 description 1
102000015336 Nerve Growth Factor Human genes 0.000 description 1
102000007072 Nerve Growth Factors Human genes 0.000 description 1
102400000064 Neuropeptide Y Human genes 0.000 description 1
102400001103 Neurotensin Human genes 0.000 description 1
101800001814 Neurotensin Proteins 0.000 description 1
108010042215 OX40 Ligand Proteins 0.000 description 1
102000002512 Orexin Human genes 0.000 description 1
108090000573 Osteocalcin Proteins 0.000 description 1
102000004067 Osteocalcin Human genes 0.000 description 1
102400000050 Oxytocin Human genes 0.000 description 1
101800000989 Oxytocin Proteins 0.000 description 1
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 1
102000003982 Parathyroid hormone Human genes 0.000 description 1
LRBQNJMCXXYXIU-PPKXGCFTSA-N Penta-digallate-beta-D-glucose Natural products OC1=C(O)C(O)=CC(C(=O)OC=2C(=C(O)C=C(C=2)C(=O)OC[C@@H]2[C@H]([C@H](OC(=O)C=3C=C(OC(=O)C=4C=C(O)C(O)=C(O)C=4)C(O)=C(O)C=3)[C@@H](OC(=O)C=3C=C(OC(=O)C=4C=C(O)C(O)=C(O)C=4)C(O)=C(O)C=3)[C@H](OC(=O)C=3C=C(OC(=O)C=4C=C(O)C(O)=C(O)C=4)C(O)=C(O)C=3)O2)OC(=O)C=2C=C(OC(=O)C=3C=C(O)C(O)=C(O)C=3)C(O)=C(O)C=2)O)=C1 LRBQNJMCXXYXIU-PPKXGCFTSA-N 0.000 description 1
108010087786 Prolactin-Releasing Hormone Proteins 0.000 description 1
102000009087 Prolactin-Releasing Hormone Human genes 0.000 description 1
102000014128 RANK Ligand Human genes 0.000 description 1
108010025832 RANK Ligand Proteins 0.000 description 1
101100288143 Rattus norvegicus Klkb1 gene Proteins 0.000 description 1
102100037422 Receptor-type tyrosine-protein phosphatase C Human genes 0.000 description 1
102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
101710205037 Sarafotoxin Proteins 0.000 description 1
102000013275 Somatomedins Human genes 0.000 description 1
108010039445 Stem Cell Factor Proteins 0.000 description 1
102000019197 Superoxide Dismutase Human genes 0.000 description 1
108010012715 Superoxide dismutase Proteins 0.000 description 1
244000269722 Thea sinensis Species 0.000 description 1
102000011923 Thyrotropin Human genes 0.000 description 1
108010061174 Thyrotropin Proteins 0.000 description 1
102000003978 Tissue Plasminogen Activator Human genes 0.000 description 1
108090000373 Tissue Plasminogen Activator Proteins 0.000 description 1
102100026890 Tumor necrosis factor ligand superfamily member 4 Human genes 0.000 description 1
102100032100 Tumor necrosis factor ligand superfamily member 8 Human genes 0.000 description 1
102100040245 Tumor necrosis factor receptor superfamily member 5 Human genes 0.000 description 1
102100036857 Tumor necrosis factor receptor superfamily member 8 Human genes 0.000 description 1
102000005789 Vascular Endothelial Growth Factors Human genes 0.000 description 1
108010019530 Vascular Endothelial Growth Factors Proteins 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
108010067390 Viral Proteins Proteins 0.000 description 1
239000003070 absorption delaying agent Substances 0.000 description 1
239000002253 acid Substances 0.000 description 1
230000002378 acidificating effect Effects 0.000 description 1
239000004480 active ingredient Substances 0.000 description 1
125000003158 alcohol group Chemical group 0.000 description 1
102000015395 alpha 1-Antitrypsin Human genes 0.000 description 1
108010050122 alpha 1-Antitrypsin Proteins 0.000 description 1
229940024142 alpha 1-antitrypsin Drugs 0.000 description 1
108010030291 alpha-Galactosidase Proteins 0.000 description 1
239000003242 anti bacterial agent Substances 0.000 description 1
230000000844 anti-bacterial effect Effects 0.000 description 1
229940121375 antifungal agent Drugs 0.000 description 1
239000003429 antifungal agent Substances 0.000 description 1
239000003963 antioxidant agent Substances 0.000 description 1
230000003078 antioxidant effect Effects 0.000 description 1
235000006708 antioxidants Nutrition 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
230000001746 atrial effect Effects 0.000 description 1
230000036765 blood level Effects 0.000 description 1
DNDCVAGJPBKION-DOPDSADYSA-N bombesin Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(N)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CC=1NC2=CC=CC=C2C=1)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H]1NC(=O)CC1)C(C)C)C1=CN=CN1 DNDCVAGJPBKION-DOPDSADYSA-N 0.000 description 1
QXZGBUJJYSLZLT-FDISYFBBSA-N bradykinin Chemical compound NC(=N)NCCC[C@H](N)C(=O)N1CCC[C@H]1C(=O)N1[C@H](C(=O)NCC(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CO)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)CCC1 QXZGBUJJYSLZLT-FDISYFBBSA-N 0.000 description 1
210000004899 c-terminal region Anatomy 0.000 description 1
201000011510 cancer Diseases 0.000 description 1
239000000969 carrier Substances 0.000 description 1
230000001413 cellular effect Effects 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
229940107137 cholecystokinin Drugs 0.000 description 1
238000000576 coating method Methods 0.000 description 1
230000000112 colonic effect Effects 0.000 description 1
229940047120 colony stimulating factors Drugs 0.000 description 1
230000001010 compromised effect Effects 0.000 description 1
238000013270 controlled release Methods 0.000 description 1
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 1
229960000258 corticotropin Drugs 0.000 description 1
238000010908 decantation Methods 0.000 description 1
239000003405 delayed action preparation Substances 0.000 description 1
230000003111 delayed effect Effects 0.000 description 1
230000004069 differentiation Effects 0.000 description 1
239000000539 dimer Substances 0.000 description 1
239000007884 disintegrant Substances 0.000 description 1
239000002612 dispersion medium Substances 0.000 description 1
239000002934 diuretic Substances 0.000 description 1
JMNJYGMAUMANNW-FIXZTSJVSA-N dynorphin a Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(O)=O)NC(=O)CNC(=O)CNC(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=CC=C1 JMNJYGMAUMANNW-FIXZTSJVSA-N 0.000 description 1
238000010894 electron beam technology Methods 0.000 description 1
238000005538 encapsulation Methods 0.000 description 1
229960002062 enfuvirtide Drugs 0.000 description 1
238000005516 engineering process Methods 0.000 description 1
230000002255 enzymatic effect Effects 0.000 description 1
229940116977 epidermal growth factor Drugs 0.000 description 1
229940105423 erythropoietin Drugs 0.000 description 1
150000002148 esters Chemical class 0.000 description 1
229960004222 factor ix Drugs 0.000 description 1
229960000301 factor viii Drugs 0.000 description 1
239000002350 fibrinopeptide Substances 0.000 description 1
229930003935 flavonoid Natural products 0.000 description 1
235000017173 flavonoids Nutrition 0.000 description 1
230000004927 fusion Effects 0.000 description 1
229940099052 fuzeon Drugs 0.000 description 1
PUBCCFNQJQKCNC-XKNFJVFFSA-N gastrin-releasingpeptide Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(N)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@H](CC(N)=O)NC(=O)CNC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)CNC(=O)[C@H](C)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC(C)C)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)C(C)C)[C@@H](C)O)C(C)C)[C@@H](C)O)C(C)C)C1=CNC=N1 PUBCCFNQJQKCNC-XKNFJVFFSA-N 0.000 description 1
230000023266 generation of precursor metabolites and energy Effects 0.000 description 1
102000018146 globin Human genes 0.000 description 1
108060003196 globin Proteins 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
239000008103 glucose Substances 0.000 description 1
239000008187 granular material Substances 0.000 description 1
235000009569 green tea Nutrition 0.000 description 1
238000000338 in vitro Methods 0.000 description 1
238000011534 incubation Methods 0.000 description 1
230000001939 inductive effect Effects 0.000 description 1
239000003112 inhibitor Substances 0.000 description 1
230000002401 inhibitory effect Effects 0.000 description 1
229940125396 insulin Drugs 0.000 description 1
108010021315 integrin beta7 Proteins 0.000 description 1
229940047122 interleukins Drugs 0.000 description 1
238000007918 intramuscular administration Methods 0.000 description 1
238000010255 intramuscular injection Methods 0.000 description 1
239000007927 intramuscular injection Substances 0.000 description 1
238000001990 intravenous administration Methods 0.000 description 1
238000010253 intravenous injection Methods 0.000 description 1
239000007951 isotonicity adjuster Substances 0.000 description 1
210000000265 leukocyte Anatomy 0.000 description 1
230000000670 limiting effect Effects 0.000 description 1
238000011068 loading method Methods 0.000 description 1
230000007774 longterm Effects 0.000 description 1
229920002521 macromolecule Polymers 0.000 description 1
OFIZOVDANLLTQD-ZVNXOKPXSA-N magainin i Chemical compound C([C@H](NC(=O)[C@H](CCCCN)NC(=O)CNC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CO)C(O)=O)C1=CC=CC=C1 OFIZOVDANLLTQD-ZVNXOKPXSA-N 0.000 description 1
239000011159 matrix material Substances 0.000 description 1
ORRDHOMWDPJSNL-UHFFFAOYSA-N melanin concentrating hormone Chemical compound N1C(=O)C(C(C)C)NC(=O)C(CCCNC(N)=N)NC(=O)CNC(=O)C(C(C)C)NC(=O)C(CCSC)NC(=O)C(NC(=O)C(CCCNC(N)=N)NC(=O)C(NC(=O)C(NC(=O)C(N)CC(O)=O)C(C)O)CCSC)CSSCC(C(=O)NC(CC=2C3=CC=CC=C3NC=2)C(=O)NC(CCC(O)=O)C(=O)NC(C(C)C)C(O)=O)NC(=O)C2CCCN2C(=O)C(CCCNC(N)=N)NC(=O)C1CC1=CC=C(O)C=C1 ORRDHOMWDPJSNL-UHFFFAOYSA-N 0.000 description 1
239000012528 membrane Substances 0.000 description 1
239000004005 microsphere Substances 0.000 description 1
230000003278 mimic effect Effects 0.000 description 1
238000012986 modification Methods 0.000 description 1
230000004048 modification Effects 0.000 description 1
SLZIZIJTGAYEKK-CIJSCKBQSA-N molport-023-220-247 Chemical compound C([C@@H](C(=O)N[C@@H](C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=1N=CNC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1N=CNC=1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(N)=O)NC(=O)[C@H]1N(CCC1)C(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)CN)[C@@H](C)O)C1=CNC=N1 SLZIZIJTGAYEKK-CIJSCKBQSA-N 0.000 description 1
230000001452 natriuretic effect Effects 0.000 description 1
HPNRHPKXQZSDFX-OAQDCNSJSA-N nesiritide Chemical compound C([C@H]1C(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CSSC[C@@H](C(=O)N1)NC(=O)CNC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CCSC)NC(=O)[C@H](CCCCN)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CO)C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1N=CNC=1)C(O)=O)=O)[C@@H](C)CC)C1=CC=CC=C1 HPNRHPKXQZSDFX-OAQDCNSJSA-N 0.000 description 1
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 1
URPYMXQQVHTUDU-OFGSCBOVSA-N nucleopeptide y Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(N)=O)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=C(O)C=C1 URPYMXQQVHTUDU-OFGSCBOVSA-N 0.000 description 1
108060005714 orexin Proteins 0.000 description 1
239000003960 organic solvent Substances 0.000 description 1
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 1
229960001723 oxytocin Drugs 0.000 description 1
239000000199 parathyroid hormone Substances 0.000 description 1
229960001319 parathyroid hormone Drugs 0.000 description 1
238000007911 parenteral administration Methods 0.000 description 1
239000008177 pharmaceutical agent Substances 0.000 description 1
238000006116 polymerization reaction Methods 0.000 description 1
229920005862 polyol Polymers 0.000 description 1
150000003077 polyols Chemical class 0.000 description 1
229920001184 polypeptide Polymers 0.000 description 1
235000013824 polyphenols Nutrition 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
GCYXWQUSHADNBF-AAEALURTSA-N preproglucagon 78-108 Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(N)=O)NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@@H](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(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](N)CC=1N=CNC=1)[C@@H](C)O)[C@@H](C)O)C(C)C)C1=CC=CC=C1 GCYXWQUSHADNBF-AAEALURTSA-N 0.000 description 1
239000002877 prolactin releasing hormone Substances 0.000 description 1
239000002461 renin inhibitor Substances 0.000 description 1
229940086526 renin-inhibitors Drugs 0.000 description 1
238000011160 research Methods 0.000 description 1
210000002345 respiratory system Anatomy 0.000 description 1
230000000717 retained effect Effects 0.000 description 1
238000012552 review Methods 0.000 description 1
210000002966 serum Anatomy 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
239000003381 stabilizer Substances 0.000 description 1
238000011146 sterile filtration Methods 0.000 description 1
230000001954 sterilising effect Effects 0.000 description 1
238000004659 sterilization and disinfection Methods 0.000 description 1
238000010254 subcutaneous injection Methods 0.000 description 1
239000007929 subcutaneous injection Substances 0.000 description 1
239000000725 suspension Substances 0.000 description 1
229940033123 tannic acid Drugs 0.000 description 1
230000001225 therapeutic effect Effects 0.000 description 1
229960000874 thyrotropin Drugs 0.000 description 1
230000001748 thyrotropin Effects 0.000 description 1
229960000187 tissue plasminogen activator Drugs 0.000 description 1
230000037317 transdermal delivery Effects 0.000 description 1
VBEQCZHXXJYVRD-GACYYNSASA-N uroanthelone Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(C)C)[C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C1=CC=C(O)C=C1 VBEQCZHXXJYVRD-GACYYNSASA-N 0.000 description 1
229960003726 vasopressin Drugs 0.000 description 1

Classifications

- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K45/00—Medicinal preparations containing active ingredients not provided for in groups A61K31/00 - A61K41/00
- A61K45/06—Mixtures of active ingredients without chemical characterisation, e.g. antiphlogistics and cardiaca
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/04—Peptides having up to 20 amino acids in a fully defined sequence; Derivatives thereof
- A61K38/08—Peptides having 5 to 11 amino acids
- 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
- A61K47/54—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 an organic compound
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K9/00—Medicinal preparations characterised by special physical form
- A61K9/0012—Galenical forms characterised by the site of application
- A61K9/0019—Injectable compositions; Intramuscular, intravenous, arterial, subcutaneous administration; Compositions to be administered through the skin in an invasive manner

Landscapes

Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Pharmacology & Pharmacy (AREA)
Veterinary Medicine (AREA)
Chemical & Material Sciences (AREA)
Public Health (AREA)
General Health & Medical Sciences (AREA)
Medicinal Chemistry (AREA)
Animal Behavior & Ethology (AREA)
Epidemiology (AREA)
Engineering & Computer Science (AREA)
Bioinformatics & Cheminformatics (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Immunology (AREA)
Gastroenterology & Hepatology (AREA)
Chemical Kinetics & Catalysis (AREA)
Organic Chemistry (AREA)
General Chemical & Material Sciences (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Medicinal Preparation (AREA)
Peptides Or Proteins (AREA)
Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)

ZA200609401A 2004-04-23 2006-11-13 Sustained release formulations ZA200609401B (en)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
US56524704P	2004-04-23	2004-04-23

Publications (1)

Publication Number	Publication Date
ZA200609401B true ZA200609401B (en)	2008-05-28

Family

ID=34967842

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
ZA200609401A ZA200609401B (en)	2004-04-23	2006-11-13	Sustained release formulations

Country Status (15)

Country	Link
US (2)	US7323169B2 (2)
EP (1)	EP1750683B1 (2)
JP (3)	JP5036533B2 (2)
KR (1)	KR101201638B1 (2)
CN (2)	CN1997356A (2)
AU (1)	AU2005237542B2 (2)
CA (1)	CA2563185C (2)
DK (1)	DK1750683T3 (2)
ES (1)	ES2400687T3 (2)
IL (1)	IL178596A (2)
PL (1)	PL1750683T3 (2)
PT (1)	PT1750683E (2)
SI (1)	SI1750683T1 (2)
WO (1)	WO2005105057A1 (2)
ZA (1)	ZA200609401B (2)

Families Citing this family (28)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
EP1750683B1 (en) *	2004-04-23	2013-01-09	Amgen Inc.	Sustained release formulations
US20050271726A1 (en) *	2004-06-02	2005-12-08	Albert Crum	Immune enhancing compositions and methods of use thereof
US7906625B2 (en)	2005-01-24	2011-03-15	Amgen Inc.	Humanized anti-amyloid antibody
US7252834B2 (en)	2005-04-25	2007-08-07	Clemson University Research Foundation (Curf)	Elastin stabilization of connective tissue
CN101258163B (zh) *	2005-06-30	2013-08-21	益普生制药股份有限公司	Glp-1药物组合物
CA2642632A1 (en) *	2006-02-15	2007-10-18	Gammacan Ltd.	Immunoglobulins from vitiligo plasma for melanoma therapy
US20090173876A1 (en) *	2006-07-21	2009-07-09	Amgen Inc.	Method of detecting and/or measuring hepcidin in a sample
US7947646B2 (en)	2007-03-06	2011-05-24	Amgen Inc.	Variant activin receptor polypeptides
EP2162540A2 (en)	2007-05-22	2010-03-17	Amgen Inc.	Compositions and methods for producing bioactive fusion proteins
EP2235058A2 (en)	2007-12-21	2010-10-06	Amgen, Inc	Anti-amyloid antibodies and uses thereof
US20090214654A1 (en) *	2008-02-21	2009-08-27	Isenburg Jason C	Treatment of aneurysm with application of connective tissue stabilization agent in combination with a delivery vehicle
US20100016833A1 (en) *	2008-07-15	2010-01-21	Ogle Matthew F	Devices for the Treatment of Vascular Aneurysm
US20100119605A1 (en) *	2008-11-12	2010-05-13	Isenburg Jason C	Compositions for tissue stabilization
US8444624B2 (en) *	2009-10-19	2013-05-21	Vatrix Medical, Inc.	Vascular medical devices with sealing elements and procedures for the treatment of isolated vessel sections
US8911468B2 (en)	2011-01-31	2014-12-16	Vatrix Medical, Inc.	Devices, therapeutic compositions and corresponding percutaneous treatment methods for aortic dissection
PH12013501865A1 (en)	2011-03-16	2014-01-06	Amgen Inc	Potent and selective inhibitors of nav1.3 and nav1.7
EP2709711B8 (en)	2011-05-18	2017-03-22	Vatrix Medical, Inc.	Coated balloons for blood vessel stabilization
HK1203384A1 (en) *	2011-12-19	2015-12-11	Amgen Inc.	Variant activin receptor polypeptides, alone or in combination with chemotherapy, and uses thereof
US20160067347A1 (en)	2012-12-20	2016-03-10	Amgen Inc.	Apj receptor agonists and uses thereof
AU2014212014A1 (en)	2013-02-01	2015-08-27	Amgen Inc.	Administration of an anti-activin-A compound to a subject
WO2014165277A2 (en)	2013-03-12	2014-10-09	Amgen Inc.	POTENT AND SELECTIVE INHIBITORS OF Nav1.7
WO2015191781A2 (en)	2014-06-10	2015-12-17	Amgen Inc.	Apelin polypeptides
TW201618783A (zh)	2014-08-07	2016-06-01	艾森塔製藥公司	以布魯頓(Bruton)氏酪胺酸激酶(BTK)佔據和BTK再合成速率為基礎之治療癌症、免疫和自體免疫疾病及發炎性疾病之方法
US11318190B2 (en)	2017-05-05	2022-05-03	United States Government As Represented By The Department Of Veterans Affairs	Methods and compositions for treating liver disease
WO2018226383A1 (en) *	2017-06-07	2018-12-13	Egy-Nano Pharma, Lp	Oral prolonged drug delivery platforms
WO2020027882A1 (en)	2018-08-03	2020-02-06	Nectero Medical, Inc.	Purified pentagalloyl glucose and devices for delivery
WO2020227437A1 (en)	2019-05-06	2020-11-12	Axial Biotherapeutics, Inc.	Sustained release solid dosage forms for modulating the colonic microbiome
CN119326891B (zh) *	2024-10-31	2025-07-01	中国人民解放军空军军医大学	Ei24激动剂以及在制备抑制食管鳞癌增殖的制剂的应用

Family Cites Families (30)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US2849370A (en) *	1953-06-04	1958-08-26	Novo Terapeutisk Labortorium A	Injectable insulin preparations with protracted effect and process of producing same
GB929406A (en)	1958-12-22	1963-06-19	Upjohn Co	A process for the production of encapsulated material
CH498653A (fr)	1968-03-29	1970-11-15	Kobayashi Takehiko	Procédé d'encapsulation de matières hydrophobes
GB2209937B (en) *	1987-09-21	1991-07-03	Depiopharm S A	Water insoluble polypeptides
US5151265A (en) *	1987-11-03	1992-09-29	Genentech, Inc.	Gamma interferon formulation
US5019400A (en) *	1989-05-01	1991-05-28	Enzytech, Inc.	Very low temperature casting of controlled release microspheres
AU5171293A (en) *	1992-10-14	1994-05-09	Regents Of The University Of Colorado, The	Ion-pairing of drugs for improved efficacy and delivery
JP2744572B2 (ja) *	1993-02-17	1998-04-28	鐘紡株式会社	ポリフェノール化合物含有皮膚外用剤組成物の変色防止方法
JPH06345668A (ja) *	1993-06-07	1994-12-20	Shibayagi:Kk	感染防御組成物およびその用途
US5922253A (en) *	1995-05-18	1999-07-13	Alkermes Controlled Therapeutics, Inc.	Production scale method of forming microparticles
WO1997007788A2 (en) *	1995-08-31	1997-03-06	Alkermes Controlled Therapeutics, Inc.	Composition for sustained release of an agent
WO1998010649A1 (en)	1996-09-13	1998-03-19	University Technology Corporation	Biocompatible cationic detergents and uses therefor
US20030190307A1 (en) *	1996-12-24	2003-10-09	Biogen, Inc.	Stable liquid interferon formulations
US6531154B1 (en) *	1997-06-10	2003-03-11	Brown University Research Foundation	Modulated release from biocompatible polymers
AU8578498A (en) *	1997-07-23	1999-02-16	Perio Products Ltd.	Tannic acid-polymer compositions for controlled release of pharmaceutical agents, particularly in the oral cavity
US6180666B1 (en)	1997-09-05	2001-01-30	Anmax, Inc.	Use of gallic acid esters to increase bioavailability of orally administered pharmaceutical compounds
US5962522A (en) *	1997-09-05	1999-10-05	Avmax, Inc.	Propyl gallate to increase bioavailability of orally administered pharmaceutical compounds
US6613358B2 (en) *	1998-03-18	2003-09-02	Theodore W. Randolph	Sustained-release composition including amorphous polymer
CA2325983C (en) *	1998-04-20	2009-02-17	Genzyme Corporation	Drug delivery of proteins from polymeric blends
JP2000080027A (ja) *	1998-09-02	2000-03-21	Taiyo Kagaku Co Ltd	徐放性製剤
US6428818B1 (en) *	1999-03-30	2002-08-06	Purdue Research Foundation	Tea catechin formulations and processes for making same
WO2001032218A1 (en)	1999-11-01	2001-05-10	University Technology Corporation	Compositions and methods for controlled-release delivery and increased potency of pharmaceuticals via hydrophobic ion-pairing
US6713506B2 (en) *	2000-10-11	2004-03-30	University Of South Florida	Tea polyphenol esters and analogs thereof for cancer prevention and treatment
US6759064B2 (en) *	2001-02-22	2004-07-06	Purdue Research Foundation	Compositions based on vanilloid-catechin synergies for prevention and treatment of cancer
JP5013152B2 (ja) *	2001-02-28	2012-08-29	株式会社ビーエムジー	蛋白質複合体形成剤
US20040142048A1 (en) *	2002-02-22	2004-07-22	Morre Dorothy M.	Compositions based on proanthocyanadin-catechin synergies for prevention and treatment of cancer
WO2004012522A1 (en)	2002-07-26	2004-02-12	Dsm Ip Assets B.V.	Compositions comprising lactoferrin
US8912174B2 (en) *	2003-04-16	2014-12-16	Mylan Pharmaceuticals Inc.	Formulations and methods for treating rhinosinusitis
US7605120B2 (en) *	2003-10-22	2009-10-20	Amgen Inc.	Antagonists of the brandykinin B1 receptor
EP1750683B1 (en) *	2004-04-23	2013-01-09	Amgen Inc.	Sustained release formulations

2005
- 2005-04-25 EP EP05742315A patent/EP1750683B1/en not_active Expired - Lifetime
- 2005-04-25 SI SI200531678T patent/SI1750683T1/sl unknown
- 2005-04-25 CN CNA2005800124592A patent/CN1997356A/zh active Pending
- 2005-04-25 PL PL05742315T patent/PL1750683T3/pl unknown
- 2005-04-25 KR KR1020067021346A patent/KR101201638B1/ko not_active Expired - Fee Related
- 2005-04-25 ES ES05742315T patent/ES2400687T3/es not_active Expired - Lifetime
- 2005-04-25 CN CN201410023256.4A patent/CN103920162B/zh not_active Expired - Fee Related
- 2005-04-25 US US11/114,473 patent/US7323169B2/en not_active Expired - Fee Related
- 2005-04-25 AU AU2005237542A patent/AU2005237542B2/en not_active Ceased
- 2005-04-25 CA CA2563185A patent/CA2563185C/en not_active Expired - Fee Related
- 2005-04-25 JP JP2007509735A patent/JP5036533B2/ja not_active Expired - Fee Related
- 2005-04-25 DK DK05742315.4T patent/DK1750683T3/da active
- 2005-04-25 WO PCT/US2005/014254 patent/WO2005105057A1/en not_active Ceased
- 2005-04-25 PT PT57423154T patent/PT1750683E/pt unknown
2006
- 2006-10-15 IL IL178596A patent/IL178596A/en not_active IP Right Cessation
- 2006-11-13 ZA ZA200609401A patent/ZA200609401B/en unknown
2007
- 2007-08-30 US US11/847,984 patent/US7732399B2/en not_active Expired - Fee Related
2011
- 2011-09-09 JP JP2011196884A patent/JP2012036194A/ja active Pending
- 2011-09-09 JP JP2011196883A patent/JP5829870B2/ja not_active Expired - Fee Related

Also Published As

Publication number	Publication date
US7323169B2 (en)	2008-01-29
WO2005105057A1 (en)	2005-11-10
CA2563185A1 (en)	2005-11-10
US20050271722A1 (en)	2005-12-08
PT1750683E (pt)	2013-01-25
DK1750683T3 (da)	2013-04-15
PL1750683T3 (pl)	2013-05-31
HK1200092A1 (en)	2015-07-31
EP1750683A1 (en)	2007-02-14
EP1750683B1 (en)	2013-01-09
JP2007534698A (ja)	2007-11-29
AU2005237542A1 (en)	2005-11-10
CN1997356A (zh)	2007-07-11
AU2005237542B2 (en)	2009-12-17
IL178596A0 (en)	2007-02-11
JP5829870B2 (ja)	2015-12-09
KR101201638B1 (ko)	2012-11-15
JP2012046520A (ja)	2012-03-08
HK1103023A1 (en)	2007-12-14
KR20070026457A (ko)	2007-03-08
ES2400687T3 (es)	2013-04-11
JP5036533B2 (ja)	2012-09-26
US7732399B2 (en)	2010-06-08
CA2563185C (en)	2010-04-20
US20070292506A1 (en)	2007-12-20
CN103920162A (zh)	2014-07-16
CN103920162B (zh)	2017-07-11
JP2012036194A (ja)	2012-02-23
SI1750683T1 (sl)	2013-04-30
IL178596A (en)	2012-06-28

Publication	Publication Date	Title
US7732399B2 (en)	2010-06-08	Sustained release formulations
KR101337797B1 (ko)	2013-12-06	지속형 인간 성장 호르몬 결합체 액상 제제
DK1397155T3 (en)	2015-12-07	Prolonged release formulation
AU2002320441B2 (en)	2008-04-03	A controlled release biodegradable gel matrix
EP1742616B1 (en)	2014-10-01	Sustained-release microspheres and methods of making and using same
AU2002320122A1 (en)	2003-06-19	Sustained release formulation
KR20090043510A (ko)	2009-05-06	펩타이드의 지속 방출 전달을 위한 약학적 조성물
KR20050083605A (ko)	2005-08-26	주사 가능한 다원성 중합체 데포트 조성물 및 이의 용도
JP2013049684A (ja)	2013-03-14	ペプチドおよびタンパク質の薬学的因子の精製および安定化
ZA200306284B (en)	2005-02-14	Catheter injectable depot compositions and uses thereof.
MX2007013213A (es)	2007-12-12	Composiciones de liberacion prolongada de peptidos biodegradables que contienen porogenos.
TW201141512A (en)	2011-12-01	Liquid formulations for long-acting erythropoietin conjugate
CA2516339A1 (en)	2004-09-02	Dispersing agent for sustained-release preparation
RS51129B (sr)	2010-10-31	Kompozicije kontrolisanog otpuštanja za inteferon na osnovu pegt/pbt blokirajućim kopolimerima
HK1103023B (en)	2013-05-31	Sustained release formulations
MXPA06012009A (es)	2007-04-20	Formulaciones de liberacion prolongada
CN101022833B (zh)	2012-01-04	甘油二棕榈酸硬脂酸酯用于提高皮下或肌肉注射制剂中的蛋白质活性成分的生物利用度的用途
HK1200092B (en)	2018-06-22	Sustained release formulations
CN113527505A (zh)	2021-10-22	一种多肽和包含该多肽的药物组合物以及它们的应用
Zhao et al.	2008	Recent US patents on protein drug formulation: 2000-2007