The twists and turns of β-peptides

被引：204

作者：

DeGrado, WF ^{[1
]}

Schneider, JP ^{[1
]}

Hamuro, Y ^{[1
]}

机构：

[1] Univ Penn, Sch Med, Johnson Res Fdn, Dept Biochem & Biophys, Philadelphia, PA 19104 USA

来源：

JOURNAL OF PEPTIDE RESEARCH | 1999年 / 54卷 / 03期

关键词：

beta-peptide; beta-amino acid; conformation; structure; helix; sheet; turn;

D O I：

10.1034/j.1399-3011.1999.00131.x

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Recently, it has been discovered that peptides composed of beta-amino acids are capable of adopting novel secondary structures demonstrating that peptides composed of alpha-amino acids are not unique in their ability to fold into well-defined structures. Cyclic as well as acyclic peptides composed of beta-amino acid residues adopt turn, helical, and sheet-like conformations. Here, we discuss the synthesis and conformational preferences of individual, substituted beta-amino acids as well as the structures that peptides composed of these residues, beta-peptides, may adopt.

引用

页码：206 / 217

页数：12

共 80 条

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