A conformationally purified α-helical peptide library

被引：29

作者：

Fujii, I ^{[1
]}

Takaoka, Y ^{[1
]}

Suzuki, K ^{[1
]}

Tanaka, T ^{[1
]}

机构：

[1] Biomol Engn Res Inst, Osaka 5650874, Japan

来源：

TETRAHEDRON LETTERS | 2001年 / 42卷 / 19期

关键词：

helix-loop helix; affinity chromatography; peptide library; immobilized metal-affinity chromatography;

D O I：

10.1016/S0040-4039(01)00382-3

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

A conformationally purified peptide library was constructed based on a unique idea combining the combinatorial library concept with de novo peptide design. This peptide library was designed to allow peptides to acquire metal-binding ability when they fold into helix-loop helix structures. Therefore, a mixture of randomized peptides was purified by immobilized metal-affinity chromatography (IMAC) to provide a library of peptides with the homogenous conformation. (C) 2001 Elsevier Science Ltd. All rights reserved.

引用

页码：3323 / 3325

页数：3

共 16 条

[1] ENGINEERED METAL-BINDING PROTEINS - PURIFICATION TO PROTEIN FOLDING [J].