JP2007531711A5 - - Google Patents
Download PDFInfo
- Publication number
- JP2007531711A5 JP2007531711A5 JP2006553254A JP2006553254A JP2007531711A5 JP 2007531711 A5 JP2007531711 A5 JP 2007531711A5 JP 2006553254 A JP2006553254 A JP 2006553254A JP 2006553254 A JP2006553254 A JP 2006553254A JP 2007531711 A5 JP2007531711 A5 JP 2007531711A5
- Authority
- JP
- Japan
- Prior art keywords
- xaa
- ala
- hpyy
- val
- pro
- Prior art date
- 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.)
- Granted
Links
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 84
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 84
- 229920001184 polypeptide Polymers 0.000 claims description 82
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims description 28
- 239000008194 pharmaceutical composition Substances 0.000 claims description 17
- -1 Val Chemical compound 0.000 claims description 14
- 208000008589 Obesity Diseases 0.000 claims description 12
- 235000020824 obesity Nutrition 0.000 claims description 12
- 238000003780 insertion Methods 0.000 claims description 11
- 230000037431 insertion Effects 0.000 claims description 11
- 150000001413 amino acids Chemical class 0.000 claims description 10
- 208000030159 metabolic disease Diseases 0.000 claims description 6
- 229920000642 polymer Polymers 0.000 claims description 4
- 208000031773 Insulin resistance syndrome Diseases 0.000 claims description 3
- 239000004472 Lysine Substances 0.000 claims description 3
- 208000011580 syndromic disease Diseases 0.000 claims description 3
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 claims description 2
- 206010012601 diabetes mellitus Diseases 0.000 claims description 2
- FUOOLUPWFVMBKG-UHFFFAOYSA-N 2-Aminoisobutyric acid Chemical compound CC(C)(N)C(O)=O FUOOLUPWFVMBKG-UHFFFAOYSA-N 0.000 claims 27
- SNDPXSYFESPGGJ-UHFFFAOYSA-N L-norVal-OH Natural products CCCC(N)C(O)=O SNDPXSYFESPGGJ-UHFFFAOYSA-N 0.000 claims 15
- UEQUQVLFIPOEMF-UHFFFAOYSA-N Mianserin Chemical compound C1C2=CC=CC=C2N2CCN(C)CC2C2=CC=CC=C21 UEQUQVLFIPOEMF-UHFFFAOYSA-N 0.000 claims 15
- IPWKGIFRRBGCJO-IMJSIDKUSA-N Ala-Ser Chemical compound C[C@H]([NH3+])C(=O)N[C@@H](CO)C([O-])=O IPWKGIFRRBGCJO-IMJSIDKUSA-N 0.000 claims 14
- 125000003275 alpha amino acid group Chemical group 0.000 claims 14
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 claims 11
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 claims 11
- UKAUYVFTDYCKQA-VKHMYHEASA-N L-homoserine Chemical compound OC(=O)[C@@H](N)CCO UKAUYVFTDYCKQA-VKHMYHEASA-N 0.000 claims 10
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 claims 10
- FSYKKLYZXJSNPZ-UHFFFAOYSA-N sarcosine Chemical compound C[NH2+]CC([O-])=O FSYKKLYZXJSNPZ-UHFFFAOYSA-N 0.000 claims 10
- BJFJQOMZCSHBMY-YUMQZZPRSA-N Met-Val Chemical compound CSCC[C@H](N)C(=O)N[C@@H](C(C)C)C(O)=O BJFJQOMZCSHBMY-YUMQZZPRSA-N 0.000 claims 5
- 108010077895 Sarcosine Proteins 0.000 claims 5
- LHUBVKCLOVALIA-HJGDQZAQSA-N Thr-Arg-Gln Chemical compound [H]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)=O LHUBVKCLOVALIA-HJGDQZAQSA-N 0.000 claims 5
- LWFWZRANSFAJDR-JSGCOSHPSA-N Trp-Val Chemical compound C1=CC=C2C(C[C@H](N)C(=O)N[C@@H](C(C)C)C(O)=O)=CNC2=C1 LWFWZRANSFAJDR-JSGCOSHPSA-N 0.000 claims 5
- 229940043230 sarcosine Drugs 0.000 claims 5
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims 4
- 125000000174 L-prolyl group Chemical group [H]N1C([H])([H])C([H])([H])C([H])([H])[C@@]1([H])C(*)=O 0.000 claims 4
- 239000002202 Polyethylene glycol Substances 0.000 claims 4
- 235000014113 dietary fatty acids Nutrition 0.000 claims 4
- 229930195729 fatty acid Natural products 0.000 claims 4
- 239000000194 fatty acid Substances 0.000 claims 4
- 150000004665 fatty acids Chemical class 0.000 claims 4
- 229920001223 polyethylene glycol Polymers 0.000 claims 4
- WPWUFUBLGADILS-WDSKDSINSA-N Ala-Pro Chemical compound C[C@H](N)C(=O)N1CCC[C@H]1C(O)=O WPWUFUBLGADILS-WDSKDSINSA-N 0.000 claims 2
- 108010016626 Dipeptides Proteins 0.000 claims 2
- AFWBWPCXSWUCLB-WDSKDSINSA-N Pro-Ser Chemical compound OC[C@@H](C([O-])=O)NC(=O)[C@@H]1CCC[NH2+]1 AFWBWPCXSWUCLB-WDSKDSINSA-N 0.000 claims 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims 2
- 108010087924 alanylproline Proteins 0.000 claims 2
- 210000004899 c-terminal region Anatomy 0.000 claims 2
- 230000001939 inductive effect Effects 0.000 claims 2
- 229920003169 water-soluble polymer Polymers 0.000 claims 2
- AWJGUZSYVIVZGP-YUMQZZPRSA-N Pro-Val Chemical compound CC(C)[C@@H](C(O)=O)NC(=O)[C@@H]1CCCN1 AWJGUZSYVIVZGP-YUMQZZPRSA-N 0.000 claims 1
- YNXLOPYTAAFMTN-SBUIBGKBSA-N C([C@H](N)C(=O)N1CCC[C@H]1C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=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](CCCNC(N)=N)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)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)C1=CC=C(O)C=C1 Chemical compound C([C@H](N)C(=O)N1CCC[C@H]1C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=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](CCCNC(N)=N)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)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)C1=CC=C(O)C=C1 YNXLOPYTAAFMTN-SBUIBGKBSA-N 0.000 description 62
- 102100029909 Peptide YY Human genes 0.000 description 41
- 108010088847 Peptide YY Proteins 0.000 description 40
- 241000700159 Rattus Species 0.000 description 18
- 210000004027 cell Anatomy 0.000 description 12
- 102000005962 receptors Human genes 0.000 description 12
- 108020003175 receptors Proteins 0.000 description 12
- 230000037396 body weight Effects 0.000 description 10
- 238000002474 experimental method Methods 0.000 description 10
- 241000699670 Mus sp. Species 0.000 description 8
- 230000000694 effects Effects 0.000 description 8
- 238000000034 method Methods 0.000 description 8
- 102100038991 Neuropeptide Y receptor type 2 Human genes 0.000 description 7
- 101710197945 Neuropeptide Y receptor type 2 Proteins 0.000 description 7
- 108010087230 Sincalide Proteins 0.000 description 7
- 238000010609 cell counting kit-8 assay Methods 0.000 description 7
- 210000000232 gallbladder Anatomy 0.000 description 7
- 238000010255 intramuscular injection Methods 0.000 description 7
- 239000007927 intramuscular injection Substances 0.000 description 7
- 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 7
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 7
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 239000000556 agonist Substances 0.000 description 6
- 238000004519 manufacturing process Methods 0.000 description 6
- 239000000203 mixture Substances 0.000 description 6
- 239000011780 sodium chloride Substances 0.000 description 6
- 206010012735 Diarrhoea Diseases 0.000 description 5
- 101710151321 Melanostatin Proteins 0.000 description 5
- 102400000064 Neuropeptide Y Human genes 0.000 description 5
- 108010079943 Pentagastrin Proteins 0.000 description 5
- 150000001875 compounds Chemical class 0.000 description 5
- 230000005764 inhibitory process Effects 0.000 description 5
- 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 5
- 229960000444 pentagastrin Drugs 0.000 description 5
- ANRIQLNBZQLTFV-DZUOILHNSA-N pentagastrin Chemical compound C([C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1[C]2C=CC=CC2=NC=1)NC(=O)CCNC(=O)OC(C)(C)C)CCSC)C(N)=O)C1=CC=CC=C1 ANRIQLNBZQLTFV-DZUOILHNSA-N 0.000 description 5
- 108091033319 polynucleotide Proteins 0.000 description 5
- 102000040430 polynucleotide Human genes 0.000 description 5
- 239000002157 polynucleotide Substances 0.000 description 5
- 238000012453 sprague-dawley rat model Methods 0.000 description 5
- 241001465754 Metazoa Species 0.000 description 4
- 206010061902 Pancreatic neoplasm Diseases 0.000 description 4
- 201000010099 disease Diseases 0.000 description 4
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 4
- 231100000673 dose–response relationship Toxicity 0.000 description 4
- 235000013305 food Nutrition 0.000 description 4
- 230000037406 food intake Effects 0.000 description 4
- 235000012631 food intake Nutrition 0.000 description 4
- 235000009200 high fat diet Nutrition 0.000 description 4
- 208000015486 malignant pancreatic neoplasm Diseases 0.000 description 4
- 201000002528 pancreatic cancer Diseases 0.000 description 4
- 208000008443 pancreatic carcinoma Diseases 0.000 description 4
- 210000002784 stomach Anatomy 0.000 description 4
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 235000001014 amino acid Nutrition 0.000 description 3
- 238000000540 analysis of variance Methods 0.000 description 3
- 230000003247 decreasing effect Effects 0.000 description 3
- 210000004211 gastric acid Anatomy 0.000 description 3
- 230000027119 gastric acid secretion Effects 0.000 description 3
- 230000030136 gastric emptying Effects 0.000 description 3
- 239000007924 injection Substances 0.000 description 3
- 238000002347 injection Methods 0.000 description 3
- 235000015097 nutrients Nutrition 0.000 description 3
- 238000001356 surgical procedure Methods 0.000 description 3
- 208000024891 symptom Diseases 0.000 description 3
- 208000001072 type 2 diabetes mellitus Diseases 0.000 description 3
- 208000024172 Cardiovascular disease Diseases 0.000 description 2
- 108020004414 DNA Proteins 0.000 description 2
- 206010012742 Diarrhoea infectious Diseases 0.000 description 2
- 208000018522 Gastrointestinal disease Diseases 0.000 description 2
- 206010020772 Hypertension Diseases 0.000 description 2
- 108010041872 Islet Amyloid Polypeptide Proteins 0.000 description 2
- 102000036770 Islet Amyloid Polypeptide Human genes 0.000 description 2
- 102000016267 Leptin Human genes 0.000 description 2
- 108010092277 Leptin Proteins 0.000 description 2
- 241000699666 Mus <mouse, genus> Species 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- 239000012980 RPMI-1640 medium Substances 0.000 description 2
- 102000004142 Trypsin Human genes 0.000 description 2
- 108090000631 Trypsin Proteins 0.000 description 2
- 230000009858 acid secretion Effects 0.000 description 2
- 239000004480 active ingredient Substances 0.000 description 2
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 2
- 201000011510 cancer Diseases 0.000 description 2
- 230000005907 cancer growth Effects 0.000 description 2
- HGAZMNJKRQFZKS-UHFFFAOYSA-N chloroethene;ethenyl acetate Chemical compound ClC=C.CC(=O)OC=C HGAZMNJKRQFZKS-UHFFFAOYSA-N 0.000 description 2
- 238000001212 derivatisation Methods 0.000 description 2
- 235000005911 diet Nutrition 0.000 description 2
- 230000037213 diet Effects 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 208000001848 dysentery Diseases 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 230000002496 gastric effect Effects 0.000 description 2
- 201000009863 inflammatory diarrhea Diseases 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- NRYBAZVQPHGZNS-ZSOCWYAHSA-N leptin Chemical compound O=C([C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](N)CC(C)C)CCSC)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CS)C(O)=O NRYBAZVQPHGZNS-ZSOCWYAHSA-N 0.000 description 2
- 229940039781 leptin Drugs 0.000 description 2
- 230000002503 metabolic effect Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 230000002265 prevention Effects 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 239000012588 trypsin Substances 0.000 description 2
- 238000005303 weighing Methods 0.000 description 2
- WNYKZOWMSHGMPJ-YGPTWXQHSA-N (4S)-5-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S,3S)-1-[[(2S)-4-amino-1-[[(2S)-1-[[(2S,3S)-1-[[(2S,3R)-1-[[(2S)-1-[[(2S)-5-amino-1-[[(2S)-1-[[(1S)-1-carboxy-2-(4-hydroxyphenyl)ethyl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-1,5-dioxopentan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1,4-dioxobutan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-3-(1H-imidazol-4-yl)-1-oxopropan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]amino]-3-hydroxy-1-oxopropan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-methylsulfanyl-1-oxobutan-2-yl]amino]-3-carboxy-1-oxopropan-2-yl]amino]-5-oxo-4-[[(2S)-2-[[(2S)-pyrrolidine-2-carbonyl]amino]propanoyl]amino]pentanoic acid Chemical compound CC[C@H](C)[C@H](NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](C)NC(=O)[C@H](CCSC)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H]1CCCN1)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](CCCN=C(N)N)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](Cc1ccc(O)cc1)C(O)=O WNYKZOWMSHGMPJ-YGPTWXQHSA-N 0.000 description 1
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- 206010052747 Adenocarcinoma pancreas Diseases 0.000 description 1
- 206010003210 Arteriosclerosis Diseases 0.000 description 1
- 206010004016 Bacterial diarrhoea Diseases 0.000 description 1
- 208000031648 Body Weight Changes Diseases 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 206010006187 Breast cancer Diseases 0.000 description 1
- 208000026310 Breast neoplasm Diseases 0.000 description 1
- 101100175010 Caenorhabditis elegans gbf-1 gene Proteins 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- VTYYLEPIZMXCLO-UHFFFAOYSA-L Calcium carbonate Chemical class [Ca+2].[O-]C([O-])=O VTYYLEPIZMXCLO-UHFFFAOYSA-L 0.000 description 1
- 241000589876 Campylobacter Species 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- 229940123158 Cannabinoid CB1 receptor antagonist Drugs 0.000 description 1
- 206010007559 Cardiac failure congestive Diseases 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 206010008631 Cholera Diseases 0.000 description 1
- 208000000668 Chronic Pancreatitis Diseases 0.000 description 1
- 241000193403 Clostridium Species 0.000 description 1
- 108700010070 Codon Usage Proteins 0.000 description 1
- 206010009944 Colon cancer Diseases 0.000 description 1
- 208000011231 Crohn disease Diseases 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 101710088194 Dehydrogenase Proteins 0.000 description 1
- 201000004624 Dermatitis Diseases 0.000 description 1
- 238000001061 Dunnett's test Methods 0.000 description 1
- 208000030814 Eating disease Diseases 0.000 description 1
- 208000019454 Feeding and Eating disease Diseases 0.000 description 1
- 208000022555 Genital disease Diseases 0.000 description 1
- 229930182566 Gentamicin Natural products 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
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Chemical group OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 206010019280 Heart failures Diseases 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101000585528 Homo sapiens Peptide YY Proteins 0.000 description 1
- 208000035150 Hypercholesterolemia Diseases 0.000 description 1
- 206010022489 Insulin Resistance Diseases 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical group SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical group OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
- 206010025476 Malabsorption Diseases 0.000 description 1
- 208000004155 Malabsorption Syndromes Diseases 0.000 description 1
- 208000023178 Musculoskeletal disease Diseases 0.000 description 1
- 102000004129 N-Type Calcium Channels Human genes 0.000 description 1
- 108090000699 N-Type Calcium Channels Proteins 0.000 description 1
- 108050002826 Neuropeptide Y Receptor Proteins 0.000 description 1
- 102000012301 Neuropeptide Y receptor Human genes 0.000 description 1
- 241001263478 Norovirus Species 0.000 description 1
- 206010033649 Pancreatitis chronic Diseases 0.000 description 1
- 229930182555 Penicillin Natural products 0.000 description 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
- 206010060862 Prostate cancer Diseases 0.000 description 1
- 208000000236 Prostatic Neoplasms Diseases 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 241000283984 Rodentia Species 0.000 description 1
- 241000702670 Rotavirus Species 0.000 description 1
- 241000607142 Salmonella Species 0.000 description 1
- 206010049416 Short-bowel syndrome Diseases 0.000 description 1
- 208000006011 Stroke Diseases 0.000 description 1
- 208000007536 Thrombosis Diseases 0.000 description 1
- 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 1
- 206010046996 Varicose vein Diseases 0.000 description 1
- 206010051511 Viral diarrhoea Diseases 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 102000030621 adenylate cyclase Human genes 0.000 description 1
- 108060000200 adenylate cyclase Proteins 0.000 description 1
- 210000000577 adipose tissue Anatomy 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- APKFDSVGJQXUKY-INPOYWNPSA-N amphotericin B Chemical compound O[C@H]1[C@@H](N)[C@H](O)[C@@H](C)O[C@H]1O[C@H]1/C=C/C=C/C=C/C=C/C=C/C=C/C=C/[C@H](C)[C@@H](O)[C@@H](C)[C@H](C)OC(=O)C[C@H](O)C[C@H](O)CC[C@@H](O)[C@H](O)C[C@H](O)C[C@](O)(C[C@H](O)[C@H]2C(O)=O)O[C@H]2C1 APKFDSVGJQXUKY-INPOYWNPSA-N 0.000 description 1
- 229940069428 antacid Drugs 0.000 description 1
- 239000003159 antacid agent Substances 0.000 description 1
- 230000001458 anti-acid effect Effects 0.000 description 1
- 230000001028 anti-proliverative effect Effects 0.000 description 1
- 230000001262 anti-secretory effect Effects 0.000 description 1
- 230000004872 arterial blood pressure Effects 0.000 description 1
- 208000011775 arteriosclerosis disease Diseases 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 208000010668 atopic eczema Diseases 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000008901 benefit Effects 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
- 230000008033 biological extinction Effects 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 230000036772 blood pressure Effects 0.000 description 1
- 230000004579 body weight change Effects 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 210000000133 brain stem Anatomy 0.000 description 1
- 210000004900 c-terminal fragment Anatomy 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 239000003555 cannabinoid 1 receptor antagonist Substances 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 201000001883 cholelithiasis Diseases 0.000 description 1
- 230000001684 chronic effect Effects 0.000 description 1
- 208000029742 colonic neoplasm Diseases 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 230000008602 contraction Effects 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Chemical group SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 208000012106 cystic neoplasm Diseases 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 208000010643 digestive system disease Diseases 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- 208000016097 disease of metabolism Diseases 0.000 description 1
- 235000014632 disordered eating Nutrition 0.000 description 1
- 239000003792 electrolyte Substances 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 238000005265 energy consumption Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000029142 excretion Effects 0.000 description 1
- 239000012091 fetal bovine serum Substances 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 208000020694 gallbladder disease Diseases 0.000 description 1
- 208000018685 gastrointestinal system disease Diseases 0.000 description 1
- 230000002178 gastroprotective effect Effects 0.000 description 1
- 238000002695 general anesthesia Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 229960002518 gentamicin Drugs 0.000 description 1
- 230000010030 glucose lowering effect Effects 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Chemical group 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 230000000004 hemodynamic effect Effects 0.000 description 1
- 210000001320 hippocampus Anatomy 0.000 description 1
- 210000003016 hypothalamus Anatomy 0.000 description 1
- 238000007455 ileostomy Methods 0.000 description 1
- 238000005286 illumination Methods 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 230000031891 intestinal absorption Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 208000002551 irritable bowel syndrome Diseases 0.000 description 1
- 210000004731 jugular vein Anatomy 0.000 description 1
- 238000002350 laparotomy Methods 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 235000015263 low fat diet Nutrition 0.000 description 1
- 230000003211 malignant effect Effects 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 108010058785 neuropeptide Y (13-36) Proteins 0.000 description 1
- 235000020925 non fasting Nutrition 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 235000021232 nutrient availability Nutrition 0.000 description 1
- 230000003204 osmotic effect Effects 0.000 description 1
- 201000008482 osteoarthritis Diseases 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 201000002094 pancreatic adenocarcinoma Diseases 0.000 description 1
- 210000000277 pancreatic duct Anatomy 0.000 description 1
- 108091005474 pancreatic polypeptide receptors Proteins 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 230000007170 pathology Effects 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 108010070727 peptide YY receptor Proteins 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-N phosphoric acid Substances OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000002335 preservative effect Effects 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 230000005180 public health Effects 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000000611 regression analysis Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000005070 sampling Methods 0.000 description 1
- 208000005893 serous cystadenoma Diseases 0.000 description 1
- UNAANXDKBXWMLN-UHFFFAOYSA-N sibutramine Chemical compound C=1C=C(Cl)C=CC=1C1(C(N(C)C)CC(C)C)CCC1 UNAANXDKBXWMLN-UHFFFAOYSA-N 0.000 description 1
- 229960004425 sibutramine Drugs 0.000 description 1
- 230000011664 signaling Effects 0.000 description 1
- 201000002859 sleep apnea Diseases 0.000 description 1
- 150000003384 small molecules Chemical group 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 235000000891 standard diet Nutrition 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 229960005322 streptomycin Drugs 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 210000003523 substantia nigra Anatomy 0.000 description 1
- 210000000225 synapse Anatomy 0.000 description 1
- 238000012353 t test Methods 0.000 description 1
- 210000001103 thalamus Anatomy 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 208000027185 varicose disease Diseases 0.000 description 1
- 230000002792 vascular Effects 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 230000003442 weekly effect Effects 0.000 description 1
- 230000004584 weight gain Effects 0.000 description 1
- 235000019786 weight gain Nutrition 0.000 description 1
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US54340704P | 2004-02-11 | 2004-02-11 | |
| US54340604P | 2004-02-11 | 2004-02-11 | |
| US60/543,407 | 2004-02-11 | ||
| US60/543,406 | 2004-02-11 | ||
| PCT/US2005/004351 WO2005077094A2 (en) | 2004-02-11 | 2005-02-11 | Pancreatic polypeptide family motifs and polypeptides comprising the same |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2007531711A JP2007531711A (ja) | 2007-11-08 |
| JP2007531711A5 true JP2007531711A5 (https=) | 2008-03-21 |
| JP5638177B2 JP5638177B2 (ja) | 2014-12-10 |
Family
ID=34864523
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2006553254A Expired - Fee Related JP5638177B2 (ja) | 2004-02-11 | 2005-02-11 | 膵臓ポリペプチドファミリーモチーフおよびそのモチーフを含むポリペプチド |
| JP2012172601A Expired - Fee Related JP5820349B2 (ja) | 2004-02-11 | 2012-08-03 | 膵臓ポリペプチドファミリーモチーフ、ポリペプチドおよびこれらを含む方法 |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2012172601A Expired - Fee Related JP5820349B2 (ja) | 2004-02-11 | 2012-08-03 | 膵臓ポリペプチドファミリーモチーフ、ポリペプチドおよびこれらを含む方法 |
Country Status (10)
| Country | Link |
|---|---|
| US (5) | US8603969B2 (https=) |
| EP (3) | EP1789440A4 (https=) |
| JP (2) | JP5638177B2 (https=) |
| CN (1) | CN101111515B (https=) |
| AU (1) | AU2005211776B2 (https=) |
| CA (1) | CA2555894A1 (https=) |
| IL (1) | IL177403A0 (https=) |
| RU (1) | RU2427586C2 (https=) |
| SG (1) | SG178746A1 (https=) |
| WO (1) | WO2005077094A2 (https=) |
Families Citing this family (52)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US8076288B2 (en) | 2004-02-11 | 2011-12-13 | Amylin Pharmaceuticals, Inc. | Hybrid polypeptides having glucose lowering activity |
| WO2005077094A2 (en) | 2004-02-11 | 2005-08-25 | Amylin Pharmaceuticals, Inc. | Pancreatic polypeptide family motifs and polypeptides comprising the same |
| RU2385878C2 (ru) | 2004-02-11 | 2010-04-10 | Амилин Фармасьютикалз, Инк. | Пептид, обладающий свойствами амилина (варианты), и его применение (варианты) |
| US7399744B2 (en) * | 2004-03-04 | 2008-07-15 | Amylin Pharmaceuticals, Inc. | Methods for affecting body composition |
| EA011860B1 (ru) * | 2004-03-17 | 2009-06-30 | 7ТиЭм ФАРМА А/С | Селективные агонисты рецептора y2 для терапевтического воздействия |
| CA2560174A1 (en) * | 2004-03-17 | 2005-09-29 | 7Tm Pharma A/S | Y4 selective receptor agonists for therapeutic interventions |
| JP2007538017A (ja) * | 2004-05-18 | 2007-12-27 | アディテック・ファルマ・アクチボラゲット | 胃腸疾患の治療のためのｐｐｙ含有組成物 |
| EP2631244A1 (en) * | 2004-10-08 | 2013-08-28 | Amylin Pharmaceuticals, Inc. | Amylin family polypeptide-6 (AFP-6) analogs and methods of making and using them |
| EP2286840A3 (en) | 2004-11-01 | 2013-09-04 | Amylin Pharmaceuticals, LLC | Treatment of obesity and related diseases |
| MX2007006830A (es) * | 2004-12-13 | 2008-02-07 | Amylin Pharmaceuticals Inc | Porciones de la familia del polipeptido pancreatico, polipeptidos y metodos que comprenden las mismas. |
| US7410949B2 (en) * | 2005-01-18 | 2008-08-12 | Hoffmann-La Roche Inc. | Neuropeptide-2 receptor (Y-2R) agonists and uses thereof |
| PA8660701A1 (es) * | 2005-02-04 | 2006-09-22 | Pfizer Prod Inc | Agonistas de pyy y sus usos |
| EP2330124B1 (en) | 2005-08-11 | 2015-02-25 | Amylin Pharmaceuticals, LLC | Hybrid polypeptides with selectable properties |
| BRPI0614649A2 (pt) | 2005-08-11 | 2011-04-12 | Amylin Pharmaceuticals Inc | polipeptìdeos hìbridos com propriedades selecionáveis |
| AU2005337116A1 (en) | 2005-09-21 | 2007-04-12 | 7Tm Pharma A/S | Y4 selective receptor agonists for therapeutic interventions |
| ATE516301T1 (de) | 2005-09-21 | 2011-07-15 | 7Tm Pharma As | Y2-selektive rezeptoragonisten für therapeutische eingriffe |
| GB0613196D0 (en) * | 2006-07-03 | 2006-08-09 | Imp Innovations Ltd | Novel compounds and their effects on feeding behaviour |
| AU2008274845A1 (en) | 2007-07-06 | 2009-01-15 | Theratechnologies Inc. | Bifunctional fusion proteins of the alpha-melanocyte stimulating hormone (alpha-MSH) and atrial natriuretic protein (ANP) and uses in hypertension and acute kidney injury |
| US20100273722A1 (en) * | 2007-08-06 | 2010-10-28 | Yale University | Modified miniature proteins |
| CN102027007A (zh) * | 2008-05-16 | 2011-04-20 | 诺沃-诺迪斯克有限公司 | 长效的y2和/或y4受体激动剂 |
| GB0817067D0 (en) * | 2008-09-18 | 2008-10-22 | 7Tm Pharma As | Intestinal treatment |
| EP2477643A1 (en) * | 2009-09-18 | 2012-07-25 | Novo Nordisk A/S | Long-acting y2 receptor agonists |
| GB201001333D0 (en) * | 2010-01-27 | 2010-03-17 | Imp Innovations Ltd | Novel compounds and their effects on feeding behaviour |
| EP2600887A4 (en) * | 2010-07-09 | 2014-01-22 | Amylin Pharmaceuticals Llc | MICROCRYSTALLINE Y RECEPTOR AGONISTS |
| MX377589B (es) | 2010-12-16 | 2025-03-10 | Novo Nordisk As | Composiciones sólidas que comprenden agonista de glp-1 y sal del ácido n-(8-(2-hidroxibenzoil)amino)caprílico. |
| US9861116B2 (en) | 2010-12-20 | 2018-01-09 | Hill's Pet Nutrition, Inc. | Pet food compositions for inducing a satiety response |
| GB201101459D0 (en) * | 2011-01-27 | 2011-03-16 | Imp Innovations Ltd | Novel compounds and thier effects on fedding behaviour |
| WO2012125622A1 (en) | 2011-03-14 | 2012-09-20 | Bristol-Myers Squibb Company | Substituted adipic acid amides and uses thereof |
| WO2013004983A1 (en) | 2011-07-04 | 2013-01-10 | Imperial Innovations Limited | Novel compounds and their effects on feeding behaviour |
| CN104203266B (zh) | 2012-03-22 | 2017-12-26 | 诺和诺德股份有限公司 | Glp‑1肽组合物及其制备 |
| UA116217C2 (uk) | 2012-10-09 | 2018-02-26 | Санофі | Пептидна сполука як подвійний агоніст рецепторів glp1-1 та глюкагону |
| HK1211232A1 (en) | 2012-12-21 | 2016-05-20 | Sanofi | Exendin-4 derivatives as dual glp1/gip or trigonal glp1/gip/glucagon agonists |
| SG11201508469YA (en) * | 2013-05-02 | 2015-11-27 | Glaxosmithkline Ip Dev Ltd | Therapeutic peptides |
| JP6672140B2 (ja) | 2013-05-02 | 2020-03-25 | ノヴォ ノルディスク アー／エス | Ｇｌｐ−１化合物の経口投薬 |
| US10583172B2 (en) | 2013-11-15 | 2020-03-10 | Novo Nordisk A/S | HPYY(1-36) having a beta-homoarginine substitution at position 35 |
| MX369818B (es) | 2013-11-15 | 2019-11-22 | Novo Nordisk As | Compuestos selectivos de peptido yy (pyy) y usos de los mismos. |
| WO2015086728A1 (en) | 2013-12-13 | 2015-06-18 | Sanofi | Exendin-4 peptide analogues as dual glp-1/gip receptor agonists |
| EP3080152A1 (en) | 2013-12-13 | 2016-10-19 | Sanofi | Non-acylated exendin-4 peptide analogues |
| WO2015086733A1 (en) | 2013-12-13 | 2015-06-18 | Sanofi | Dual glp-1/glucagon receptor agonists |
| TW201609799A (zh) | 2013-12-13 | 2016-03-16 | 賽諾菲公司 | 雙重ｇｌｐ－１／ｇｉｐ受體促效劑 |
| TW201625668A (zh) | 2014-04-07 | 2016-07-16 | 賽諾菲公司 | 作為胜肽性雙重ｇｌｐ－１／昇糖素受體激動劑之艾塞那肽－４衍生物 |
| TW201625669A (zh) | 2014-04-07 | 2016-07-16 | 賽諾菲公司 | 衍生自艾塞那肽－４（Ｅｘｅｎｄｉｎ－４）之肽類雙重ＧＬＰ－１／升糖素受體促效劑 |
| TW201625670A (zh) | 2014-04-07 | 2016-07-16 | 賽諾菲公司 | 衍生自ｅｘｅｎｄｉｎ－４之雙重ｇｌｐ－１／升糖素受體促效劑 |
| US9932381B2 (en) | 2014-06-18 | 2018-04-03 | Sanofi | Exendin-4 derivatives as selective glucagon receptor agonists |
| AR105319A1 (es) | 2015-06-05 | 2017-09-27 | Sanofi Sa | Profármacos que comprenden un conjugado agonista dual de glp-1 / glucagón conector ácido hialurónico |
| MA43205A (fr) | 2015-06-12 | 2018-09-19 | Novo Nordisk As | Composés pyy sélectifs et leurs utilisations |
| AR105284A1 (es) | 2015-07-10 | 2017-09-20 | Sanofi Sa | Derivados de exendina-4 como agonistas peptídicos duales específicos de los receptores de glp-1 / glucagón |
| JOP20190095A1 (ar) | 2016-10-27 | 2019-04-28 | Janssen Pharmaceutica Nv | مركبات ببتيد تيروسين-تيروسين الحلقية كمعدلات لمستقبلات الببتيد العصبي y |
| GB201720188D0 (en) | 2017-12-04 | 2018-01-17 | Imperial Innovations Ltd | Analogues of PYY |
| PL3746111T3 (pl) | 2018-02-02 | 2024-01-15 | Novo Nordisk A/S | Stałe kompozycje zawierające agonistę glp-1 i sól kwasu n-(8-(2- hydroksybenzoilo)amino kaprylowego i substancję poślizgową |
| US11780900B2 (en) | 2018-04-25 | 2023-10-10 | Janssen Sciences Ireland Unlimited Company | Glucagon like peptide 1 (GLP-1) fusion peptide coupled cyclic peptide tyrosine tyrosine conjugates and uses thereof |
| WO2023097363A1 (en) * | 2021-11-30 | 2023-06-08 | Garvan Institute Of Medical Research | Improved binding proteins and uses thereof |
Family Cites Families (83)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DK371079A (da) | 1978-09-28 | 1980-03-29 | Nordisk Insulinlab | Therapeutisk aktive polypeptider eller syreadditionssalte derr af og fr&mgangsmaade til fremstilling af saadanne forbindelse |
| US4391909A (en) | 1979-03-28 | 1983-07-05 | Damon Corporation | Microcapsules containing viable tissue cells |
| US4353888A (en) | 1980-12-23 | 1982-10-12 | Sefton Michael V | Encapsulation of live animal cells |
| JPS58140024A (ja) | 1982-02-15 | 1983-08-19 | Eisai Co Ltd | セクレチンの精製方法 |
| US6936694B1 (en) | 1982-05-06 | 2005-08-30 | Intermune, Inc. | Manufacture and expression of large structural genes |
| EP0094099B1 (en) | 1982-05-12 | 1986-08-27 | Aktiebolaget Iro | Loom control system |
| US4891357A (en) | 1985-02-11 | 1990-01-02 | University Of Florida | Methods and compositions for stimulation of appetite |
| US4683202A (en) | 1985-03-28 | 1987-07-28 | Cetus Corporation | Process for amplifying nucleic acid sequences |
| US4683195A (en) | 1986-01-30 | 1987-07-28 | Cetus Corporation | Process for amplifying, detecting, and/or-cloning nucleic acid sequences |
| US4839343A (en) | 1987-03-13 | 1989-06-13 | Debiopharm, S.A. | Preparation containing hexatriacontapeptides and methods of use |
| WO1989001967A1 (en) | 1987-09-03 | 1989-03-09 | Brown University Research Foundation | Blood purification with cultured renal cells |
| US4892538A (en) | 1987-11-17 | 1990-01-09 | Brown University Research Foundation | In vivo delivery of neurotransmitters by implanted, encapsulated cells |
| US5106627A (en) | 1987-11-17 | 1992-04-21 | Brown University Research Foundation | Neurological therapy devices |
| US5158881A (en) | 1987-11-17 | 1992-10-27 | Brown University Research Foundation | Method and system for encapsulating cells in a tubular extrudate in separate cell compartments |
| JP2796388B2 (ja) | 1988-05-13 | 1998-09-10 | アムジエン・インコーポレーテツド | Ｇ−ｃｓｆの精製方法 |
| US5011472A (en) | 1988-09-06 | 1991-04-30 | Brown University Research Foundation | Implantable delivery system for biological factors |
| EP0401384B1 (en) | 1988-12-22 | 1996-03-13 | Kirin-Amgen, Inc. | Chemically modified granulocyte colony stimulating factor |
| US5459039A (en) | 1989-05-12 | 1995-10-17 | Duke University | Methods for mapping genetic mutations |
| FI916066A0 (fi) | 1989-06-21 | 1991-12-20 | Univ Brown Res Found | Neurologiskt vaordsystem. |
| WO1991010470A1 (en) | 1990-01-08 | 1991-07-25 | Brown University Research Foundation | Devices and methods for enhanced delivery of active factors |
| US5149543A (en) | 1990-10-05 | 1992-09-22 | Massachusetts Institute Of Technology | Ionically cross-linked polymeric microcapsules |
| US6391343B1 (en) | 1991-01-15 | 2002-05-21 | Hemosphere, Inc. | Fibrinogen-coated particles for therapeutic use |
| HU222249B1 (hu) | 1991-03-08 | 2003-05-28 | Amylin Pharmaceuticals Inc. | Eljárás amilin agonista peptidszármazékok és ezeket tartalmazó gyógyszerkészítmények előállítására |
| JPH06133731A (ja) | 1992-10-23 | 1994-05-17 | Zenetsukusu Kk | ダイエット食品 |
| CA2153387A1 (en) | 1993-01-07 | 1994-07-21 | Hubert Koester | Dna sequencing by mass spectrometry |
| SK121895A3 (en) | 1993-03-29 | 1996-10-02 | Univ Cincinnati | Analogues of peptide yy and uses thereof |
| US5498531A (en) | 1993-09-10 | 1996-03-12 | President And Fellows Of Harvard College | Intron-mediated recombinant techniques and reagents |
| US5545549A (en) | 1994-02-03 | 1996-08-13 | Synaptic Pharmaceutical Corporation | DNA encoding a human neuropeptide Y/peptide YY (Y2) receptor and uses thereof |
| US5824784A (en) | 1994-10-12 | 1998-10-20 | Amgen Inc. | N-terminally chemically modified protein compositions and methods |
| US5696093A (en) | 1994-10-28 | 1997-12-09 | Crc For Biopharmaceutical Research Pty Limited | Method of treating nasal congestion using neuropeptide Y Y2 agonist peptides |
| US5574010A (en) | 1994-11-14 | 1996-11-12 | The Regents Of The University Of California | Treatment of pancreatic tumors with peptide YY and analogs thereof |
| US5602024A (en) | 1994-12-02 | 1997-02-11 | Synaptic Pharmaceutical Corporation | DNA encoding a hypothalamic atypical neuropeptide Y/peptide YY receptor (Y5) and uses thereof |
| US5912227A (en) | 1995-01-27 | 1999-06-15 | North Carolina State University | Method of enhancing nutrient uptake |
| US20020094346A1 (en) | 1995-05-17 | 2002-07-18 | M. D. Henry C. Lin | Method and compositions for improving digestion and absorption in the small intestine |
| US6558708B1 (en) | 1995-05-17 | 2003-05-06 | Cedars-Sinai Medical Center | Methods for manipulating upper gastrointestinal transit, blood flow, and satiety, and for treating visceral hyperalgesia |
| US5739106A (en) | 1995-06-07 | 1998-04-14 | Rink; Timothy J. | Appetite regulating compositions |
| US5980945A (en) | 1996-01-16 | 1999-11-09 | Societe De Conseils De Recherches Et D'applications Scientifique S.A. | Sustained release drug formulations |
| EP0910578A2 (en) | 1996-01-19 | 1999-04-28 | The Board Of Regents, The University Of Texas System | Recombinant expression of proteins from secretory cell lines |
| US6355478B1 (en) | 1996-06-17 | 2002-03-12 | Eli Lilly And Company | Rhesus monkey neuropeptide Y Y2 receptor |
| US5686511A (en) | 1996-06-28 | 1997-11-11 | The Valspar Corporation | Esterifying epoxy resin with carboxyl polymer and quenching |
| CA2271788A1 (en) * | 1996-11-13 | 1998-05-22 | University Of Cincinnati | Analogs of peptide yy and uses thereof |
| WO1998028427A1 (en) | 1996-12-20 | 1998-07-02 | Amgen Inc. | Ob fusion protein compositions and methods |
| EP0910565A1 (en) | 1997-02-14 | 1999-04-28 | Bayer Corporation | Amide derivatives as selective neuropeptide y receptor antagonists |
| EP0992239B1 (en) | 1997-04-23 | 2003-03-12 | Banyu Pharmaceutical Co., Ltd. | Neuropeptide y receptor antagonist |
| CA2299425A1 (en) | 1997-08-08 | 1999-02-18 | Amylin Pharmaceuticals, Inc. | Novel exendin agonist compounds |
| JP3036480B2 (ja) | 1997-08-25 | 2000-04-24 | 日本電気株式会社 | バーコード読取装置およびその焦点制御方法 |
| AU9185598A (en) | 1997-09-25 | 1999-04-12 | Banyu Pharmaceutical Co., Ltd. | Novel neuropeptide y receptor antagonists |
| ATE383867T1 (de) | 1997-11-14 | 2008-02-15 | Amylin Pharmaceuticals Inc | Neuartige exendin agonisten |
| WO1999025727A2 (en) | 1997-11-14 | 1999-05-27 | Amylin Pharmaceuticals, Inc. | Novel exendin agonist compounds |
| US6046167A (en) * | 1998-03-25 | 2000-04-04 | University Of Cincinnati | Peptide YY analogs |
| US6013622A (en) | 1998-04-15 | 2000-01-11 | Nutriceutical Technology Corporation | Method of regulating appetite and metabolism |
| AU5027299A (en) | 1998-07-31 | 2000-02-28 | Novo Nordisk A/S | Use of glp-1 and analogues for preventing type ii diabetes |
| DE60045030D1 (de) * | 1999-02-10 | 2010-11-11 | Curis Inc | Peptid yy (pyy) zur behandlung von glukose stoffwechselkrankheiten |
| US7745216B2 (en) | 1999-02-10 | 2010-06-29 | Curis, Inc. | Methods and reagents for treating glucose metabolic disorders |
| CA2373035A1 (en) | 1999-05-05 | 2000-11-16 | Scott Dax | 3a,4,5,9b-tetrahydro-1h-benz[e]indol-2-yl amine-derived neuropeptide y receptors ligands useful in the treatment of obesity and other disorders |
| PT1105409E (pt) * | 1999-05-17 | 2006-07-31 | Conjuchem Inc | Proteccao de peptidos terapeuticos endogenos da actividade de peptidases por conjugacao a componentes do sangue |
| US6506724B1 (en) | 1999-06-01 | 2003-01-14 | Amylin Pharmaceuticals, Inc. | Use of exendins and agonists thereof for the treatment of gestational diabetes mellitus |
| US6420535B1 (en) * | 1999-06-07 | 2002-07-16 | Abbott Laboratories | 6-O-carbamate ketolide derivatives |
| US6528486B1 (en) | 1999-07-12 | 2003-03-04 | Zealand Pharma A/S | Peptide agonists of GLP-1 activity |
| US6569832B1 (en) | 1999-11-12 | 2003-05-27 | Novo Nordisk A/S | Inhibition of beta cell degeneration |
| CA2396157A1 (en) | 2000-01-10 | 2001-07-19 | Amylin Pharmaceuticals, Inc. | Use of exendins and agonists thereof for modulation of triglyceride levels and treatment of dyslipidemia |
| US6734166B1 (en) | 2000-02-08 | 2004-05-11 | North Carolina State University | Method of reducing aluminum levels in the central nervous system |
| US6531478B2 (en) | 2000-02-24 | 2003-03-11 | Cheryl P. Kordik | Amino pyrazole derivatives useful for the treatment of obesity and other disorders |
| US6420352B1 (en) | 2000-07-19 | 2002-07-16 | W. Roy Knowles | Hair loss prevention |
| WO2002010195A2 (en) * | 2000-08-02 | 2002-02-07 | Theratechnologies Inc. | Modified peptides with increased potency |
| BR0116024A (pt) | 2000-12-07 | 2005-12-13 | Lilly Co Eli | Proteìna de fusão heteróloga e uso da mesma |
| US8273713B2 (en) * | 2000-12-14 | 2012-09-25 | Amylin Pharmaceuticals, Llc | Methods of treating obesity using PYY[3-36] |
| JP3935487B2 (ja) * | 2001-07-16 | 2007-06-20 | フーベルト・ケスター | 捕獲化合物、その収集物、ならびにプロテオームおよび複合組成物の分析方法 |
| EP1411968B1 (en) | 2001-07-31 | 2008-09-17 | THE GOVERNMENT OF THE UNITED STATES OF AMERICA, as represented by THE SECRETARY, DEPARTMENT OF HEALTH AND HUMAN SERVICES | Glp-1 exendin-4 peptide analogs and uses thereof |
| KR100989647B1 (ko) * | 2001-09-24 | 2010-10-26 | 오레곤 헬스 앤드 사이언스 유니버시티 | 식습관의 변화 |
| AU2002364587A1 (en) * | 2001-12-21 | 2003-07-30 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| EP2261250B1 (en) * | 2001-12-21 | 2015-07-01 | Human Genome Sciences, Inc. | GCSF-Albumin fusion proteins |
| EP1474163A2 (en) | 2002-01-10 | 2004-11-10 | Imperial College Innovations Limited | Modification of feeding behavior |
| US6861236B2 (en) * | 2002-05-24 | 2005-03-01 | Applied Nanosystems B.V. | Export and modification of (poly)peptides in the lantibiotic way |
| ATE494002T1 (de) | 2002-06-14 | 2011-01-15 | Amylin Pharmaceuticals Inc | Prävention und/oder behandlung von colitis ulcerosa mit pyy oder pyyä3-36ü |
| WO2003105736A1 (ja) | 2002-06-17 | 2003-12-24 | Mori Atsuo | 局所冷却カテーテルおよびそれを用いた局所冷却デバイス |
| US7192922B2 (en) | 2002-11-19 | 2007-03-20 | Allegheny-Singer Research Institute | Method of treating left ventricular dysfunction |
| AU2003297356A1 (en) | 2002-12-17 | 2004-07-14 | Amylin Pharmaceuticals, Inc. | Prevention and treatment of cardiac arrhythmias |
| US7166575B2 (en) | 2002-12-17 | 2007-01-23 | Nastech Pharmaceutical Company Inc. | Compositions and methods for enhanced mucosal delivery of peptide YY and methods for treating and preventing obesity |
| US20070027073A1 (en) | 2003-04-08 | 2007-02-01 | Menachem Rubinstein | Long-acting derivatives of pyy agonists |
| WO2005077094A2 (en) | 2004-02-11 | 2005-08-25 | Amylin Pharmaceuticals, Inc. | Pancreatic polypeptide family motifs and polypeptides comprising the same |
| MX2007006830A (es) * | 2004-12-13 | 2008-02-07 | Amylin Pharmaceuticals Inc | Porciones de la familia del polipeptido pancreatico, polipeptidos y metodos que comprenden las mismas. |
| US8236933B2 (en) * | 2005-04-13 | 2012-08-07 | Garvan Institute Of Medical Research | Modified animal lacking functional PYY gene, monoclonal antibodies that bind PYY isoforms and uses therefor |
-
2005
- 2005-02-11 WO PCT/US2005/004351 patent/WO2005077094A2/en not_active Ceased
- 2005-02-11 EP EP05722950A patent/EP1789440A4/en not_active Withdrawn
- 2005-02-11 AU AU2005211776A patent/AU2005211776B2/en not_active Ceased
- 2005-02-11 CA CA002555894A patent/CA2555894A1/en not_active Abandoned
- 2005-02-11 US US11/055,098 patent/US8603969B2/en not_active Expired - Fee Related
- 2005-02-11 EP EP20100013143 patent/EP2335716A3/en not_active Withdrawn
- 2005-02-11 JP JP2006553254A patent/JP5638177B2/ja not_active Expired - Fee Related
- 2005-02-11 EP EP10013127.5A patent/EP2335715A3/en not_active Withdrawn
- 2005-12-12 CN CN2005800471988A patent/CN101111515B/zh not_active Expired - Fee Related
- 2005-12-12 SG SG2012007761A patent/SG178746A1/en unknown
- 2005-12-12 RU RU2007126653/04A patent/RU2427586C2/ru not_active IP Right Cessation
- 2005-12-12 US US11/301,744 patent/US7723471B2/en not_active Expired - Fee Related
-
2006
- 2006-08-10 IL IL177403A patent/IL177403A0/en unknown
-
2009
- 2009-12-17 US US12/640,352 patent/US8426361B2/en not_active Expired - Fee Related
-
2012
- 2012-08-03 JP JP2012172601A patent/JP5820349B2/ja not_active Expired - Fee Related
-
2013
- 2013-04-08 US US13/858,398 patent/US8906849B2/en not_active Expired - Fee Related
-
2014
- 2014-11-12 US US14/539,540 patent/US20150231204A1/en not_active Abandoned
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP2007531711A5 (https=) | ||
| US9441023B2 (en) | Peptide YY analogs | |
| JP6563614B1 (ja) | アシル化ｇｌｐ−１／ｇｌｐ−２二重アゴニスト | |
| JP6898231B2 (ja) | Ｇｉｐアゴニスト化合物及び方法 | |
| TWI670281B (zh) | Ｇｉｐ－ｇｌｐ－１雙重促效劑化合物及方法 | |
| AU2014345570B2 (en) | Glucagon-GLP-1-GIP triple agonist compounds | |
| JP5820349B2 (ja) | 膵臓ポリペプチドファミリーモチーフ、ポリペプチドおよびこれらを含む方法 | |
| AU2008257448B2 (en) | Unacylated ghrelin as therapeutic agent in the treatment of metabolic disorders | |
| US11713344B2 (en) | Acylated oxyntomodulin peptide analog | |
| AU2014345569A1 (en) | GIP-GLP-1 dual agonist compounds and methods | |
| JP2020500890A (ja) | Ｇｌｐ−１／ｇｌｐ−２二重アゴニスト | |
| TW201202265A (en) | Glucagon analogues | |
| CN103003300A (zh) | Glp-1受体激动剂和胃泌素的肽缀合物及其用途 | |
| CN102292347A (zh) | 胰高血糖素类似物 | |
| WO2019201328A1 (zh) | 酰化的glp-1衍生物 | |
| CN116970062B (zh) | 一种超长效glp-1多肽衍生物及其制备方法和用途 | |
| JP2023144098A (ja) | ポリペプチドを含む医薬組成物 | |
| WO2019201333A1 (zh) | Glp-1衍生物及其治疗用途 | |
| CA3043151C (en) | Acylated glp-1/glp-2 dual agonists |