Inhibition of amyloid fibril formation by peptide analogues modified with α-aminoisobutyric acid

被引：119

作者：

Gilead, S ^{[1
]}

Gazit, E ^{[1
]}

机构：

[1] Tel Aviv Univ, Dept Mol Microbiol & Biotechnol, IL-69978 Tel Aviv, Israel

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2004年 / 43卷 / 31期

关键词：

amyloid fibrils; islet amyloid polypeptide; peptides; protein folding; self assembly;

D O I：

10.1002/anie.200353565

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Breaking up is not hard to do with an α-aminoisobutyric (Aib) acid β-breaker, which has a remarkably restricted conformation. A novel approach to the inhibition of amyloid formation was developed that uses peptides modified with Aib (see figure). The similarity of Aib to hydrophobic amino acids, often found in amyloidogenic sequences, allows its integration into recognition motifs.

引用

页码：4041 / 4044

页数：4

共 36 条

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