Induction of Unexpected Left-Handed Helicity by an N-Terminal L-Amino Acid in an Otherwise Achiral Peptide Chain

被引：78

作者：

Brown, Robert A. ^{[1
]}

Marcelli, Tommaso ^{[1
,2
]}

De Poli, Matteo ^{[1
]}

Sola, Jordi ^{[1
]}

Clayden, Jonathan ^{[1
]}

机构：

[1] Univ Manchester, Sch Chem, Manchester M13 9PL, Lancs, England

[2] Politecn Milan, Dipartimento Chim Mat & Ingn Chim Giulio Natta, I-20131 Milan, Italy

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2012年 / 51卷 / 06期

基金：

英国工程与自然科学研究理事会; 英国生物技术与生命科学研究理事会;

关键词：

circular dichroism; conformation analysis; foldamers; helical structures; peptides; SCREW-SENSE PREFERENCE; CIRCULAR-DICHROISM; CHIRAL INDUCTION; PROTEIN; CONFORMATION; AIB; COMMUNICATION; INFORMATION; ASSIGNMENT; MOLECULES;

D O I：

10.1002/anie.201107583

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Peptide helices containing L-amino acids are typically right-handed. Exceptions are peptide helices containing the achiral amino acids 2-aminoisobutyric acid and glycine with a single chiral amino acid at the Nterminus. These helices are left-handed when the N-terminal residue is a common tertiary proteinogenic amino acid, such as L-valine (see picture, left), but right-handed when the N-terminal residue is the quaternary amino acid L-α-methylvaline (right). Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：1395 / 1399

页数：5

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