JP2005529186A5 - - Google Patents
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- JP2005529186A5 JP2005529186A5 JP2004513428A JP2004513428A JP2005529186A5 JP 2005529186 A5 JP2005529186 A5 JP 2005529186A5 JP 2004513428 A JP2004513428 A JP 2004513428A JP 2004513428 A JP2004513428 A JP 2004513428A JP 2005529186 A5 JP2005529186 A5 JP 2005529186A5
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- JP
- Japan
- Prior art keywords
- seq
- ligation
- shows
- present
- fragment
- 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
- RMVRSNDYEFQCLF-UHFFFAOYSA-N thiophenol Chemical compound SC1=CC=CC=C1 RMVRSNDYEFQCLF-UHFFFAOYSA-N 0.000 description 18
- 239000012634 fragment Substances 0.000 description 12
- 108090000765 processed proteins & peptides Proteins 0.000 description 10
- 102000015636 Oligopeptides Human genes 0.000 description 9
- 108010038807 Oligopeptides Proteins 0.000 description 9
- 238000006243 chemical reaction Methods 0.000 description 7
- 230000015572 biosynthetic process Effects 0.000 description 5
- -1 carboxy ester Chemical class 0.000 description 5
- 238000004007 reversed phase HPLC Methods 0.000 description 5
- 238000003786 synthesis reaction Methods 0.000 description 5
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 4
- 102100022068 Serine palmitoyltransferase 1 Human genes 0.000 description 4
- 101710122478 Serine palmitoyltransferase 1 Proteins 0.000 description 4
- 238000003776 cleavage reaction Methods 0.000 description 4
- 125000000623 heterocyclic group Chemical group 0.000 description 4
- 238000004128 high performance liquid chromatography Methods 0.000 description 4
- 239000011347 resin Substances 0.000 description 4
- 229920005989 resin Polymers 0.000 description 4
- 230000007017 scission Effects 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- 150000007970 thio esters Chemical class 0.000 description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 3
- 150000001413 amino acids Chemical group 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 125000006297 carbonyl amino group Chemical group [H]N([*:2])C([*:1])=O 0.000 description 3
- 150000002148 esters Chemical group 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 102000004196 processed proteins & peptides Human genes 0.000 description 3
- 230000002194 synthesizing effect Effects 0.000 description 3
- NXFFJDQHYLNEJK-UHFFFAOYSA-N 2-[4-[(4-chlorophenyl)methyl]-7-fluoro-5-methylsulfonyl-2,3-dihydro-1h-cyclopenta[b]indol-3-yl]acetic acid Chemical compound C1=2C(S(=O)(=O)C)=CC(F)=CC=2C=2CCC(CC(O)=O)C=2N1CC1=CC=C(Cl)C=C1 NXFFJDQHYLNEJK-UHFFFAOYSA-N 0.000 description 2
- VHYFNPMBLIVWCW-UHFFFAOYSA-N 4-Dimethylaminopyridine Chemical compound CN(C)C1=CC=NC=C1 VHYFNPMBLIVWCW-UHFFFAOYSA-N 0.000 description 2
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 2
- 101800005149 Peptide B Proteins 0.000 description 2
- 102100028899 Spermatid nuclear transition protein 1 Human genes 0.000 description 2
- 235000001014 amino acid Nutrition 0.000 description 2
- 229940024606 amino acid Drugs 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 210000004027 cell Anatomy 0.000 description 2
- 235000018417 cysteine Nutrition 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 125000006575 electron-withdrawing group Chemical group 0.000 description 2
- 229960000789 guanidine hydrochloride Drugs 0.000 description 2
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- 238000004949 mass spectrometry Methods 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 108010091748 peptide A Proteins 0.000 description 2
- 229920001184 polypeptide Polymers 0.000 description 2
- 125000006239 protecting group Chemical group 0.000 description 2
- 235000018102 proteins Nutrition 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 2
- 238000007086 side reaction Methods 0.000 description 2
- 238000001542 size-exclusion chromatography Methods 0.000 description 2
- 229910000162 sodium phosphate Inorganic materials 0.000 description 2
- 239000001488 sodium phosphate Substances 0.000 description 2
- 108010044129 spermatid transition proteins Proteins 0.000 description 2
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 2
- ZBPUWGDUVAAWJY-QHCPKHFHSA-N (2s)-2-(9h-fluoren-9-ylmethoxycarbonylamino)-3-[hydroxy(phenylmethoxy)phosphoryl]oxypropanoic acid Chemical compound C([C@@H](C(=O)O)NC(=O)OCC1C2=CC=CC=C2C2=CC=CC=C21)OP(O)(=O)OCC1=CC=CC=C1 ZBPUWGDUVAAWJY-QHCPKHFHSA-N 0.000 description 1
- 125000003088 (fluoren-9-ylmethoxy)carbonyl group Chemical group 0.000 description 1
- PQHQBRJAAZQXHL-GQCOAOBCSA-N 2-(4-iodanyl-2,5-dimethoxyphenyl)ethanamine Chemical compound COC1=CC(CCN)=C(OC)C=C1[125I] PQHQBRJAAZQXHL-GQCOAOBCSA-N 0.000 description 1
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 1
- 229960000549 4-dimethylaminophenol Drugs 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- OBMZMSLWNNWEJA-XNCRXQDQSA-N C1=CC=2C(C[C@@H]3NC(=O)[C@@H](NC(=O)[C@H](NC(=O)N(CC#CCN(CCCC[C@H](NC(=O)[C@@H](CC4=CC=CC=C4)NC3=O)C(=O)N)CC=C)NC(=O)[C@@H](N)C)CC3=CNC4=C3C=CC=C4)C)=CNC=2C=C1 Chemical compound C1=CC=2C(C[C@@H]3NC(=O)[C@@H](NC(=O)[C@H](NC(=O)N(CC#CCN(CCCC[C@H](NC(=O)[C@@H](CC4=CC=CC=C4)NC3=O)C(=O)N)CC=C)NC(=O)[C@@H](N)C)CC3=CNC4=C3C=CC=C4)C)=CNC=2C=C1 OBMZMSLWNNWEJA-XNCRXQDQSA-N 0.000 description 1
- KXDHJXZQYSOELW-UHFFFAOYSA-N Carbamic acid Chemical compound NC(O)=O KXDHJXZQYSOELW-UHFFFAOYSA-N 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- LSDPWZHWYPCBBB-UHFFFAOYSA-N Methanethiol Chemical compound SC LSDPWZHWYPCBBB-UHFFFAOYSA-N 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 101710176384 Peptide 1 Proteins 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 125000002252 acyl group Chemical group 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 125000001797 benzyl group Chemical group [H]C1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])* 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
- 150000003857 carboxamides Chemical class 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 230000008034 disappearance Effects 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000007717 exclusion Effects 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
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- 125000005647 linker group Chemical group 0.000 description 1
- 229930182817 methionine Natural products 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
- 239000008363 phosphate buffer Substances 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 238000000746 purification 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
- 238000006467 substitution reaction Methods 0.000 description 1
- TUQOTMZNTHZOKS-UHFFFAOYSA-N tributylphosphine Chemical compound CCCCP(CCCC)CCCC TUQOTMZNTHZOKS-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
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 true JP2005529186A5 (https=) | 2006-03-09 |
| JP4559219B2 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 |
| CA2612274A1 (en) * | 2005-06-16 | 2006-12-21 | 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 |
| WO2007100358A2 (en) * | 2005-10-07 | 2007-09-07 | University Of Chicago | Convergent synthesis of proteins by kinetically controlled ligation |
| US8404804B2 (en) | 2007-08-28 | 2013-03-26 | Ipsen Pharma S.A.S. | Methods and intermediates for chemical synthesis of polypeptides and proteins |
| 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 |
| JP2018528164A (ja) | 2015-07-02 | 2018-09-27 | ノーバス・インターナショナル・インコーポレイテッドＮｏｖｕｓ Ｉｎｔｅｒｎａｔｉｏｎａｌ，Ｉｎｃ． | 陰イオン界面活性剤 |
| US10584306B2 (en) | 2017-08-11 | 2020-03-10 | Board Of Regents Of The University Of Oklahoma | Surfactant microemulsions |
| WO2022143532A1 (zh) * | 2020-12-28 | 2022-07-07 | 江苏金斯瑞生物科技有限公司 | 一种肽硫酯及其首尾酰胺环肽的合成方法 |
Family Cites Families (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU745094B2 (en) * | 1997-06-13 | 2002-03-14 | Gryphon Sciences | Solid phase native chemical ligation of unprotected or N-terminal cysteine protected peptides in aqueous solution |
| KR20030046389A (ko) * | 2000-09-01 | 2003-06-12 | 그리폰 테라퓨틱스, 인코포레이티드 | 친핵체에 안정한 티오에스테르 발생 화합물, 제조 및 사용방법 |
| KR20030057529A (ko) * | 2000-09-08 | 2003-07-04 | 그리폰 테라퓨틱스, 인코포레이티드 | 합성 적혈구생성 자극 단백질 |
| BR0113623A (pt) * | 2000-09-08 | 2004-06-22 | Gryphon Therapeutics Inc | Proteìnas sintéticas de estìmulo da eritropoiese |
| GB0113657D0 (en) * | 2001-06-05 | 2001-07-25 | Geneprot Inc | Improved native chemical ligation with three or more components |
-
2003
- 2003-06-09 US US10/516,118 patent/US7781488B2/en not_active Expired - Fee Related
- 2003-06-09 EP EP03760111A patent/EP1529056B1/en not_active Expired - Lifetime
- 2003-06-09 WO PCT/IB2003/005087 patent/WO2003106615A2/en not_active Ceased
- 2003-06-09 AT AT03760111T patent/ATE458745T1/de not_active IP Right Cessation
- 2003-06-09 ES ES03760111T patent/ES2340376T3/es not_active Expired - Lifetime
- 2003-06-09 CA CA002487342A patent/CA2487342A1/en not_active Abandoned
- 2003-06-09 DE DE60331437T patent/DE60331437D1/de not_active Expired - Lifetime
- 2003-06-09 JP JP2004513428A patent/JP4559219B2/ja not_active Expired - Fee Related
- 2003-06-10 AU AU2003276286A patent/AU2003276286A1/en not_active Abandoned
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