Two helical conformations from a single foldamer backbone:: "Split personality" in short α/β-peptides

被引：191

作者：

Hayen, A

Schmitt, MA

Ngassa, FN

Thomasson, KA

Gellman, SH

机构：

[1] Univ Wisconsin, Dept Chem, Madison, WI 53706 USA

[2] Univ N Dakota, Dept Chem, Grand Forks, ND 58202 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2004年 / 43卷 / 04期

关键词：

alpha-amino acids; beta-amino acids; foldamers; helical structures; NMR spectroscopy;

D O I：

10.1002/anie.200352125

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Oligopeptides with heterogenous backbones, i.e., oligopeptides containing more than one monomer type, may be a fruitful source of new foldamers. This conclusion was suggested by studies on oligomers comprising L-α-amino acid and cyclic β-amino acid residues in a sequentially alternating pattern, which are shown to display helical secondary structure in solution.

引用

页码：505 / 510

页数：6

共 34 条

[31]

Schinnerl M, 2003, EUR J ORG CHEM, V2003, P721

[32] beta-peptides: Synthesis by Arndt-Eistert homologation with concomitant peptide coupling. Structure determination by NMR and CD spectroscopy and by X-ray crystallography. Helical secondary structure of a beta-hexapeptide in solution and its stability towards pepsin [J].