Synthesis of a designed transmembrane protein by thioether ligation of solubilised segments:: Nα-haloacetylated peptides survived resin cleavage using TFA with EDT as scavenger

被引：10

作者：

Englebretsen, DR

Choma, CT

Robillard, GT

机构：

[1] Univ Groningen, Dept Biochem, NL-9747 AG Groningen, Netherlands

[2] Univ Penn, Dept Biochem & Biophys, Philadelphia, PA 19104 USA

来源：

TETRAHEDRON LETTERS | 1998年 / 39卷 / 27期

关键词：

solid phase synthesis; peptides; cleavage reactions;

D O I：

10.1016/S0040-4039(98)00898-3

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

N alpha-haloacetylated peptides made by Fmoc solid phase synthesis survived cleavage when EDT was used as a cleavage component. Two segments of a designed transmembrane protein, one bromoacetylated, the other containing a cysteine, and each bearing a "solubilising tail" peptide, were synthesised by Fmoc SPPS. The two peptides were joined via thioether ligation. (C) 1998 Elsevier Science Ltd. All rights reserved.

引用

页码：4929 / 4932

页数：4

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