Peptide bond formation mediated by 4,5-dimethoxy-2-mercaptobenzylamine after periodate oxidation of the N-terminal serine residue

被引：65

作者：

Kawakami, T ^{[1
]}

Akaji, K ^{[1
]}

Aimoto, S ^{[1
]}

机构：

[1] Osaka Univ, Inst Prot Res, Suita, Osaka 5650871, Japan

来源：

ORGANIC LETTERS | 2001年 / 3卷 / 09期

关键词：

D O I：

10.1021/ol0157813

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

[GRAPHICS] A thiol linker-attached peptide was prepared from a nonprotected peptide via an N-alpha-alpha -oxoacyl peptide. Selective oxidation of the N-terminal serine with sodium periodate gave the N-alpha-glyoxyloyl peptide, reductive amination of which with 4,5-dimethoxy-2-(triphenylmethylthio)benzylamine gave an N-alpha-4,5-dimethoxy-2-mercaptobenzyl glycyl peptide after removal of the trityl group. The N-alpha-4,5-dimethoxy-2-mercaptobenzyl peptide can be condensed with a peptide thioester, and the linker is removable. This strategy provides a useful method for the synthesis of peptides using recombinant proteins.

引用

页码：1403 / 1405

页数：3

共 22 条

[1]

Aimoto S, 1999, BIOPOLYMERS, V51, P247, DOI 10.1002/(SICI)1097-0282(1999)51:4<247::AID-BIP2>3.0.CO

[2]

2-W

[3] Native chemical ligation using removable Nα-(1-phenyl-2-mercaptoethyl) auxiliaries [J].