JP4559219B2 - 化学連結による収束性タンパク質合成のための開裂後硫黄脱保護 - Google Patents
化学連結による収束性タンパク質合成のための開裂後硫黄脱保護 Download PDFInfo
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- JP4559219B2 JP4559219B2 JP2004513428A JP2004513428A JP4559219B2 JP 4559219 B2 JP4559219 B2 JP 4559219B2 JP 2004513428 A JP2004513428 A JP 2004513428A JP 2004513428 A JP2004513428 A JP 2004513428A JP 4559219 B2 JP4559219 B2 JP 4559219B2
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- 125000002228 disulfide group Chemical group 0.000 description 1
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
- 239000000975 dye Chemical group 0.000 description 1
- 238000002330 electrospray ionisation mass spectrometry Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- DNJIEGIFACGWOD-UHFFFAOYSA-N ethanethiol Chemical compound CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 1
- 125000004705 ethylthio group Chemical group C(C)S* 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 125000001153 fluoro group Chemical group F* 0.000 description 1
- 150000003948 formamides Chemical class 0.000 description 1
- 125000002485 formyl group Chemical group [H]C(*)=O 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 229960004198 guanidine Drugs 0.000 description 1
- 125000005179 haloacetyl group Chemical group 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 150000002429 hydrazines Chemical class 0.000 description 1
- 150000007857 hydrazones Chemical class 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 125000003453 indazolyl group Chemical group N1N=C(C2=C1C=CC=C2)* 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 239000013067 intermediate product Substances 0.000 description 1
- 125000002346 iodo group Chemical group I* 0.000 description 1
- 125000000959 isobutyl group Chemical group [H]C([H])([H])C([H])(C([H])([H])[H])C([H])([H])* 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 1
- 239000004310 lactic acid Substances 0.000 description 1
- 235000014655 lactic acid Nutrition 0.000 description 1
- 150000002632 lipids Chemical group 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 238000001906 matrix-assisted laser desorption--ionisation mass spectrometry Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 238000012775 microarray technology Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- UXOUKMQIEVGVLY-UHFFFAOYSA-N morin Natural products OC1=CC(O)=CC(C2=C(C(=O)C3=C(O)C=C(O)C=C3O2)O)=C1 UXOUKMQIEVGVLY-UHFFFAOYSA-N 0.000 description 1
- 125000004573 morpholin-4-yl group Chemical group N1(CCOCC1)* 0.000 description 1
- 238000007040 multi-step synthesis reaction Methods 0.000 description 1
- 125000001624 naphthyl group Chemical group 0.000 description 1
- 238000006386 neutralization reaction Methods 0.000 description 1
- 230000003472 neutralizing effect Effects 0.000 description 1
- 229910017604 nitric acid Inorganic materials 0.000 description 1
- 125000004433 nitrogen atom Chemical group N* 0.000 description 1
- 239000010502 orange oil Substances 0.000 description 1
- 239000012074 organic phase Substances 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 238000005897 peptide coupling reaction Methods 0.000 description 1
- 125000005062 perfluorophenyl group Chemical group FC1=C(C(=C(C(=C1F)F)F)F)* 0.000 description 1
- 230000010412 perfusion Effects 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 229910000073 phosphorus hydride Inorganic materials 0.000 description 1
- 230000000704 physical effect Effects 0.000 description 1
- 125000004193 piperazinyl group Chemical group 0.000 description 1
- 125000003386 piperidinyl group Chemical group 0.000 description 1
- 229920002647 polyamide Polymers 0.000 description 1
- 229920006122 polyamide resin Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 229920005990 polystyrene resin Polymers 0.000 description 1
- 230000008092 positive effect Effects 0.000 description 1
- 230000001124 posttranscriptional effect Effects 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- 235000010333 potassium nitrate Nutrition 0.000 description 1
- 239000004323 potassium nitrate Substances 0.000 description 1
- 238000002953 preparative HPLC Methods 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 125000001436 propyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- HNJBEVLQSNELDL-UHFFFAOYSA-N pyrrolidin-2-one Chemical compound O=C1CCCN1 HNJBEVLQSNELDL-UHFFFAOYSA-N 0.000 description 1
- 125000001567 quinoxalinyl group Chemical group N1=C(C=NC2=CC=CC=C12)* 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 238000006462 rearrangement reaction Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000006722 reduction reaction Methods 0.000 description 1
- 125000006413 ring segment Chemical group 0.000 description 1
- 239000012047 saturated solution Substances 0.000 description 1
- 150000003335 secondary amines Chemical group 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 235000017557 sodium bicarbonate Nutrition 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate Nutrition 0.000 description 1
- 239000008259 solid foam Substances 0.000 description 1
- 238000010532 solid phase synthesis reaction Methods 0.000 description 1
- 238000004611 spectroscopical analysis Methods 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 239000011550 stock solution Substances 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 125000002653 sulfanylmethyl group Chemical group [H]SC([H])([H])[*] 0.000 description 1
- 125000004434 sulfur atom Chemical group 0.000 description 1
- 239000003930 superacid Substances 0.000 description 1
- XBXCNNQPRYLIDE-UHFFFAOYSA-N tert-butylcarbamic acid Chemical compound CC(C)(C)NC(O)=O XBXCNNQPRYLIDE-UHFFFAOYSA-N 0.000 description 1
- 125000005931 tert-butyloxycarbonyl group Chemical group [H]C([H])([H])C(OC(*)=O)(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- TXEYQDLBPFQVAA-UHFFFAOYSA-N tetrafluoromethane Chemical compound FC(F)(F)F TXEYQDLBPFQVAA-UHFFFAOYSA-N 0.000 description 1
- 125000003718 tetrahydrofuranyl group Chemical group 0.000 description 1
- 125000005958 tetrahydrothienyl group Chemical group 0.000 description 1
- WROMPOXWARCANT-UHFFFAOYSA-N tfa trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F.OC(=O)C(F)(F)F WROMPOXWARCANT-UHFFFAOYSA-N 0.000 description 1
- RSPCKAHMRANGJZ-UHFFFAOYSA-N thiohydroxylamine Chemical compound SN RSPCKAHMRANGJZ-UHFFFAOYSA-N 0.000 description 1
- 150000003583 thiosemicarbazides Chemical class 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- JQZIKLPHXXBMCA-UHFFFAOYSA-N triphenylmethanethiol Chemical compound C=1C=CC=CC=1C(C=1C=CC=CC=1)(S)C1=CC=CC=C1 JQZIKLPHXXBMCA-UHFFFAOYSA-N 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 238000000825 ultraviolet detection Methods 0.000 description 1
- 238000010518 undesired secondary reaction Methods 0.000 description 1
- 125000005500 uronium group Chemical group 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
- C07K1/1072—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides by covalent attachment of residues or functional groups
- C07K1/1077—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides by covalent attachment of residues or functional groups by covalent attachment of residues other than amino acids or peptide residues, e.g. sugars, polyols, fatty acids
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/02—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length in solution
- C07K1/026—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length in solution by fragment condensation in solution
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/04—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length on carriers
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
- C07K7/06—Linear peptides containing only normal peptide links having 5 to 11 amino acids
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Analytical Chemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US38780302P | 2002-06-10 | 2002-06-10 | |
| US40753002P | 2002-08-30 | 2002-08-30 | |
| PCT/IB2003/005087 WO2003106615A2 (en) | 2002-06-10 | 2003-06-09 | Post-cleavage sulfur deprotection for convergent protein synthesis by chemical ligation |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2005529186A JP2005529186A (ja) | 2005-09-29 |
| JP2005529186A5 JP2005529186A5 (https=) | 2006-03-09 |
| JP4559219B2 true JP4559219B2 (ja) | 2010-10-06 |
Family
ID=29739962
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2004513428A Expired - Fee Related JP4559219B2 (ja) | 2002-06-10 | 2003-06-09 | 化学連結による収束性タンパク質合成のための開裂後硫黄脱保護 |
Country Status (9)
| Country | Link |
|---|---|
| US (1) | US7781488B2 (https=) |
| EP (1) | EP1529056B1 (https=) |
| JP (1) | JP4559219B2 (https=) |
| AT (1) | ATE458745T1 (https=) |
| AU (1) | AU2003276286A1 (https=) |
| CA (1) | CA2487342A1 (https=) |
| DE (1) | DE60331437D1 (https=) |
| ES (1) | ES2340376T3 (https=) |
| WO (1) | WO2003106615A2 (https=) |
Families Citing this family (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR2877946B1 (fr) * | 2004-11-12 | 2011-02-11 | Commissariat Energie Atomique | Peptides derives de la maurocalcine utilisables comme vecteurs pour l'adressage intracellulaire de molecules d'interet |
| EP1904515B1 (en) * | 2005-06-16 | 2010-12-08 | Amylin Pharmaceuticals, Inc. | Side-chain extended ligation |
| EP1770099A1 (en) * | 2005-09-28 | 2007-04-04 | University of Geneva | Method of producing a modified (poly)peptide |
| US7674881B2 (en) * | 2005-10-07 | 2010-03-09 | The University Of Chicago | Convergent synthesis of proteins by kinetically controlled ligation |
| JP2010537984A (ja) * | 2007-08-28 | 2010-12-09 | イプセン ファルマ ソシエテ パール アクシオン サンプリフィエ | ポリペプチドおよび蛋白質の化学合成のための方法および中間体 |
| EP2197895A4 (en) * | 2007-09-04 | 2012-12-26 | Ipsen Pharma Sas | METHODS AND INTERMEDIATES FOR CHEMICAL SYNTHESIS OF POLYPEPTIDES AND PROTEINS |
| US9175053B2 (en) | 2010-02-09 | 2015-11-03 | Ben-Gurion University Of The Negev Research And Development Authority | Chemical preparation of ubiquitin thioesters and modifications thereof |
| PL3317390T3 (pl) | 2015-07-02 | 2021-04-19 | Novus International Inc. | Anionowe środki powierzchniowo czynne |
| US10584306B2 (en) | 2017-08-11 | 2020-03-10 | Board Of Regents Of The University Of Oklahoma | Surfactant microemulsions |
| US20240076311A1 (en) * | 2020-12-28 | 2024-03-07 | Jiangsu Genscript Biotech Co., Ltd. | Method for synthesizing peptide thioesters and head-to-tail amide cyclic peptide thereof |
Family Cites Families (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ATE285415T1 (de) * | 1997-06-13 | 2005-01-15 | Gryphon Therapeutics Inc | Festphasige native chemische ligation von ungeschützten oder n-cystein-geschützten peptiden in wässrigen lösungen |
| KR20030046389A (ko) * | 2000-09-01 | 2003-06-12 | 그리폰 테라퓨틱스, 인코포레이티드 | 친핵체에 안정한 티오에스테르 발생 화합물, 제조 및 사용방법 |
| BR0113579A (pt) * | 2000-09-08 | 2003-06-17 | Gryphon Therapeutics Inc | Proteìnas sintéticas modificadas por polìmero |
| EE200300089A (et) * | 2000-09-08 | 2005-02-15 | Gryphon Therapeutics, Inc. | Sünteetilised erütropoeesi stimuleerivad valgud, nende valmistamismeetodid ning kasutamine |
| GB0113657D0 (en) * | 2001-06-05 | 2001-07-25 | Geneprot Inc | Improved native chemical ligation with three or more components |
-
2003
- 2003-06-09 ES ES03760111T patent/ES2340376T3/es not_active Expired - Lifetime
- 2003-06-09 WO PCT/IB2003/005087 patent/WO2003106615A2/en not_active Ceased
- 2003-06-09 JP JP2004513428A patent/JP4559219B2/ja not_active Expired - Fee Related
- 2003-06-09 CA CA002487342A patent/CA2487342A1/en not_active Abandoned
- 2003-06-09 AT AT03760111T patent/ATE458745T1/de not_active IP Right Cessation
- 2003-06-09 DE DE60331437T patent/DE60331437D1/de not_active Expired - Lifetime
- 2003-06-09 EP EP03760111A patent/EP1529056B1/en not_active Expired - Lifetime
- 2003-06-09 US US10/516,118 patent/US7781488B2/en not_active Expired - Fee Related
- 2003-06-10 AU AU2003276286A patent/AU2003276286A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| AU2003276286A1 (en) | 2003-12-31 |
| EP1529056B1 (en) | 2010-02-24 |
| WO2003106615A2 (en) | 2003-12-24 |
| ES2340376T3 (es) | 2010-06-02 |
| ATE458745T1 (de) | 2010-03-15 |
| EP1529056A2 (en) | 2005-05-11 |
| US7781488B2 (en) | 2010-08-24 |
| DE60331437D1 (de) | 2010-04-08 |
| CA2487342A1 (en) | 2003-12-24 |
| WO2003106615A3 (en) | 2004-09-16 |
| US20070059792A1 (en) | 2007-03-15 |
| JP2005529186A (ja) | 2005-09-29 |
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