ITCS20140016A1 - - Google Patents
Download PDFInfo
- Publication number
- ITCS20140016A1 ITCS20140016A1 ITCS20140016A ITCS20140016A1 IT CS20140016 A1 ITCS20140016 A1 IT CS20140016A1 IT CS20140016 A ITCS20140016 A IT CS20140016A IT CS20140016 A1 ITCS20140016 A1 IT CS20140016A1
- Authority
- IT
- Italy
- Prior art keywords
- leptin
- tetrapeptide
- amino acids
- peptide
- amino acid
- Prior art date
Links
- 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 claims description 68
- 102000016267 Leptin Human genes 0.000 claims description 66
- 108010092277 Leptin Proteins 0.000 claims description 66
- 229940039781 leptin Drugs 0.000 claims description 66
- 239000005557 antagonist Substances 0.000 claims description 18
- 150000001413 amino acids Chemical class 0.000 claims description 17
- 229920001223 polyethylene glycol Polymers 0.000 claims description 15
- 235000001014 amino acid Nutrition 0.000 claims description 12
- 229940024606 amino acid Drugs 0.000 claims description 12
- 235000004279 alanine Nutrition 0.000 claims description 7
- 238000001727 in vivo Methods 0.000 claims description 7
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 claims description 6
- 239000002202 Polyethylene glycol Substances 0.000 claims description 6
- 229960000310 isoleucine Drugs 0.000 claims description 5
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 claims description 4
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 claims description 4
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 claims description 4
- 230000003042 antagnostic effect Effects 0.000 claims description 4
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 claims description 4
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 claims description 3
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 claims description 3
- 235000003704 aspartic acid Nutrition 0.000 claims description 3
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 claims description 3
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 claims description 3
- 210000004881 tumor cell Anatomy 0.000 claims description 3
- 125000001433 C-terminal amino-acid group Chemical group 0.000 claims description 2
- 230000004614 tumor growth Effects 0.000 claims description 2
- 230000005751 tumor progression Effects 0.000 claims description 2
- 210000004216 mammary stem cell Anatomy 0.000 claims 1
- 210000004027 cell Anatomy 0.000 description 35
- 108090000765 processed proteins & peptides Proteins 0.000 description 30
- 108090000623 proteins and genes Proteins 0.000 description 15
- 206010028980 Neoplasm Diseases 0.000 description 12
- 238000003556 assay Methods 0.000 description 12
- 235000018102 proteins Nutrition 0.000 description 10
- 102000004169 proteins and genes Human genes 0.000 description 10
- 102400001368 Epidermal growth factor Human genes 0.000 description 9
- 101800003838 Epidermal growth factor Proteins 0.000 description 9
- 241000699670 Mus sp. Species 0.000 description 9
- 229940116977 epidermal growth factor Drugs 0.000 description 9
- 102000005962 receptors Human genes 0.000 description 9
- 108020003175 receptors Proteins 0.000 description 9
- 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 9
- 230000000694 effects Effects 0.000 description 8
- 238000003119 immunoblot Methods 0.000 description 8
- 239000000284 extract Substances 0.000 description 7
- 229920001817 Agar Polymers 0.000 description 6
- 206010006187 Breast cancer Diseases 0.000 description 6
- 101150046735 LEPR gene Proteins 0.000 description 6
- 101150063827 LEPROT gene Proteins 0.000 description 6
- 230000009471 action Effects 0.000 description 6
- 230000004913 activation Effects 0.000 description 6
- 239000008272 agar Substances 0.000 description 6
- 230000001404 mediated effect Effects 0.000 description 6
- 230000026731 phosphorylation Effects 0.000 description 6
- 238000006366 phosphorylation reaction Methods 0.000 description 6
- 208000026310 Breast neoplasm Diseases 0.000 description 5
- 102000043136 MAP kinase family Human genes 0.000 description 5
- 108091054455 MAP kinase family Proteins 0.000 description 5
- 238000000134 MTT assay Methods 0.000 description 5
- 231100000002 MTT assay Toxicity 0.000 description 5
- 108091008611 Protein Kinase B Proteins 0.000 description 5
- 102100033810 RAC-alpha serine/threonine-protein kinase Human genes 0.000 description 5
- 102000005861 leptin receptors Human genes 0.000 description 5
- 108010019813 leptin receptors Proteins 0.000 description 5
- 102000004196 processed proteins & peptides Human genes 0.000 description 5
- 238000004458 analytical method Methods 0.000 description 4
- 230000002401 inhibitory effect Effects 0.000 description 4
- 238000012546 transfer Methods 0.000 description 4
- 102100031181 Glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 3
- 108010017324 STAT3 Transcription Factor Proteins 0.000 description 3
- 102100024040 Signal transducer and activator of transcription 3 Human genes 0.000 description 3
- 239000000556 agonist Substances 0.000 description 3
- 230000010261 cell growth Effects 0.000 description 3
- 230000009087 cell motility Effects 0.000 description 3
- 238000001516 cell proliferation assay Methods 0.000 description 3
- 108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 description 3
- 238000000338 in vitro Methods 0.000 description 3
- 230000037361 pathway Effects 0.000 description 3
- 238000003757 reverse transcription PCR Methods 0.000 description 3
- 230000019491 signal transduction Effects 0.000 description 3
- 101000997832 Homo sapiens Tyrosine-protein kinase JAK2 Proteins 0.000 description 2
- 102100033444 Tyrosine-protein kinase JAK2 Human genes 0.000 description 2
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 2
- 230000001093 anti-cancer Effects 0.000 description 2
- 239000002246 antineoplastic agent Substances 0.000 description 2
- 229940041181 antineoplastic drug Drugs 0.000 description 2
- 238000004166 bioassay Methods 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 230000037396 body weight Effects 0.000 description 2
- 230000004663 cell proliferation Effects 0.000 description 2
- 230000009089 cytolysis Effects 0.000 description 2
- 230000001086 cytosolic effect Effects 0.000 description 2
- 230000007423 decrease Effects 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- 201000002491 encephalomyelitis Diseases 0.000 description 2
- 102000015694 estrogen receptors Human genes 0.000 description 2
- 108010038795 estrogen receptors Proteins 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 239000003102 growth factor Substances 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 108020004999 messenger RNA Proteins 0.000 description 2
- JTJMJGYZQZDUJJ-UHFFFAOYSA-N phencyclidine Chemical compound C1CCCCN1C1(C=2C=CC=CC=2)CCCCC1 JTJMJGYZQZDUJJ-UHFFFAOYSA-N 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 230000003827 upregulation Effects 0.000 description 2
- 101100346171 Arabidopsis thaliana MORC3 gene Proteins 0.000 description 1
- 208000023275 Autoimmune disease Diseases 0.000 description 1
- 101100168604 Candida albicans (strain SC5314 / ATCC MYA-2876) CRH12 gene Proteins 0.000 description 1
- 208000005623 Carcinogenesis Diseases 0.000 description 1
- 208000001333 Colorectal Neoplasms Diseases 0.000 description 1
- 108010058546 Cyclin D1 Proteins 0.000 description 1
- 102100024165 G1/S-specific cyclin-D1 Human genes 0.000 description 1
- 101100168607 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) UTR2 gene Proteins 0.000 description 1
- 210000001789 adipocyte Anatomy 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 230000036528 appetite Effects 0.000 description 1
- 235000019789 appetite Nutrition 0.000 description 1
- 238000011717 athymic nude mouse Methods 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 210000000481 breast Anatomy 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 230000036952 cancer formation Effects 0.000 description 1
- 231100000504 carcinogenesis Toxicity 0.000 description 1
- 230000006369 cell cycle progression Effects 0.000 description 1
- 230000003833 cell viability Effects 0.000 description 1
- 108091092328 cellular RNA Proteins 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 210000003169 central nervous system Anatomy 0.000 description 1
- 206010009887 colitis Diseases 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 231100000673 dose–response relationship Toxicity 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 210000003016 hypothalamus Anatomy 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 239000007928 intraperitoneal injection Substances 0.000 description 1
- DVCSNHXRZUVYAM-BQBZGAKWSA-N leu-asp Chemical compound CC(C)C[C@H](N)C(=O)N[C@H](C(O)=O)CC(O)=O DVCSNHXRZUVYAM-BQBZGAKWSA-N 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 238000000034 method Methods 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 108091005601 modified peptides Proteins 0.000 description 1
- 230000004899 motility Effects 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 230000008506 pathogenesis Effects 0.000 description 1
- 230000006320 pegylation Effects 0.000 description 1
- 239000000813 peptide hormone Substances 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- 238000011170 pharmaceutical development Methods 0.000 description 1
- 108091005981 phosphorylated proteins Proteins 0.000 description 1
- 239000000902 placebo Substances 0.000 description 1
- 229940068196 placebo Drugs 0.000 description 1
- 230000004983 pleiotropic effect Effects 0.000 description 1
- 230000016833 positive regulation of signal transduction Effects 0.000 description 1
- 238000004393 prognosis Methods 0.000 description 1
- 230000002062 proliferating effect Effects 0.000 description 1
- 230000009822 protein phosphorylation Effects 0.000 description 1
- 239000000018 receptor agonist Substances 0.000 description 1
- 229940044601 receptor agonist Drugs 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 206010039073 rheumatoid arthritis Diseases 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/10—Tetrapeptides
- C07K5/1002—Tetrapeptides with the first amino acid being neutral
- C07K5/1005—Tetrapeptides with the first amino acid being neutral and aliphatic
- C07K5/1008—Tetrapeptides with the first amino acid being neutral and aliphatic the side chain containing 0 or 1 carbon atoms, i.e. Gly, Ala
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/10—Tetrapeptides
- C07K5/1002—Tetrapeptides with the first amino acid being neutral
- C07K5/1005—Tetrapeptides with the first amino acid being neutral and aliphatic
- C07K5/101—Tetrapeptides with the first amino acid being neutral and aliphatic the side chain containing 2 to 4 carbon atoms, e.g. Val, Ile, Leu
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Life Sciences & Earth Sciences (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| ITCS20140016 IT1423968B1 (enExample) | 2014-04-28 | 2014-04-28 |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| ITCS20140016 IT1423968B1 (enExample) | 2014-04-28 | 2014-04-28 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| ITCS20140016A1 true ITCS20140016A1 (enExample) | 2015-10-28 |
| IT1423968B1 IT1423968B1 (enExample) | 2016-08-26 |
Family
ID=50943385
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ITCS20140016 IT1423968B1 (enExample) | 2014-04-28 | 2014-04-28 |
Country Status (1)
| Country | Link |
|---|---|
| IT (1) | IT1423968B1 (enExample) |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2006056987A2 (en) * | 2004-11-26 | 2006-06-01 | Yissum Research Development Company Of The Hebrew University Of Jerusalem | Leptin antagonists |
-
2014
- 2014-04-28 IT ITCS20140016 patent/IT1423968B1/it active
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2006056987A2 (en) * | 2004-11-26 | 2006-06-01 | Yissum Research Development Company Of The Hebrew University Of Jerusalem | Leptin antagonists |
Non-Patent Citations (1)
| Title |
|---|
| NISHIUCHI Y ET AL: "Combined solid-phase and solution approach to protein synthesis", PEPTIDE SCIENCE: PRESENT AND FUTURE, PROCEEDINGS OF THE INTERNATIONAL PEPTIDE SYMPOSIUM, 1ST, KYOTO, NOV. 30-DEC. 5, 1997, KLUWER, DORDRECHT, NL, 1 January 1999 (1999-01-01), pages 490 - 494, XP008165968, ISBN: 0-7923-5271-8 * |
Also Published As
| Publication number | Publication date |
|---|---|
| IT1423968B1 (enExample) | 2016-08-26 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Denais et al. | Nuclear mechanics in cancer | |
| Henstridge et al. | Minireview: recent developments in the physiology and pathology of the lysophosphatidylinositol-sensitive receptor GPR55 | |
| Liu et al. | The oxytocin receptor signalling system and breast cancer: a critical review | |
| Abukhdeir et al. | P21 and p27: roles in carcinogenesis and drug resistance | |
| Yamaki et al. | Rel A/p65 is required for cytokine-induced myotube atrophy | |
| CN113769114A (zh) | 癌症模型及相关方法 | |
| KR20170058424A (ko) | 펩티드모방 거대고리 및 이의 용도 | |
| WO2020171113A1 (ja) | Ｆｇｆｒ１変異陽性脳腫瘍を治療するための医薬組成物及び治療方法 | |
| JP2023010979A (ja) | 疾患及び障害の治療のためのｎｆカッパｂ活性の阻害剤 | |
| Park et al. | Neuromedin B receptor antagonism inhibits migration, invasion, and epithelial-mesenchymal transition of breast cancer cells | |
| Shukla et al. | A novel peptidomimetic therapeutic for selective suppression of lung cancer stem cells over non-stem cancer cells | |
| CA2890108C (en) | Method for treating prostate cancer | |
| EP3187191B1 (en) | Antibody for recognizing specific motif of wls protein, and pharmaceutical composition containing same | |
| KR20140116060A (ko) | 의학적 용도 | |
| ITCS20140016A1 (enExample) | ||
| JP2022140789A (ja) | Ｍｅｎａプロテインアイソフォームキナーゼを標的とする抗がん療法のための方法及び組成物 | |
| Zhang et al. | Role of SIP30 in the development and maintenance of peripheral nerve injury-induced neuropathic pain | |
| JP7676323B2 (ja) | Ｇｐｃｒヘテロマー阻害剤及びその使用 | |
| Yong et al. | Kinetic characterization of an intestinal trefoil factor receptor | |
| Bose et al. | 5-hydroxytryptamine and enterochromaffin cells in the irritable bowel syndrome | |
| EP4025585A1 (en) | Modified peptides and associated methods of use | |
| Yang et al. | Nucleophosmin 1 associating with engulfment and cell motility protein 1 regulates hepatocellular carcinoma cell chemotaxis and metastasis | |
| Wang et al. | Involvement of adrenomedullin in the attenuation of acute morphine-induced analgesia in rats | |
| Vincent-Mistiaen | Epithelial-mesenchymal transition links inflammation and fibrosis in the pathogenesis of endometriosis: a narrative review | |
| EP2986989A1 (en) | Compositions and methods for inhibiting chemoresistance in cancer and improving response to therapy |