Design of Highly Stabilized β-Hairpin Peptides through Cation-π Interactions of Lysine and N-Methyllysine with an Aromatic Pockets

被引：45

作者：

Riemen, Alexander J. ^{[1
]}

Waters, Marcey L. ^{[1
]}

机构：

[1] Univ N Carolina, Dept Chem, Chapel Hill, NC 27599 USA

来源：

BIOCHEMISTRY | 2009年 / 48卷 / 07期

基金：

美国国家卫生研究院;

关键词：

MODEL; QUANTIFICATION; CHROMODOMAIN; RECOGNITION; METHYLATION; POSITION;

D O I：

10.1021/bi801706k

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Two tryptophan residues were incorporated on one face of a beta-hairpin peptide to form an aromatic pocket that interacts with a lysine or N-methylated lysine via cation-pi interactions. The two tryptophan residues were found to pack against the lysine side chain forming an aromatic pocket similar to those observed in trimethylated lysine receptor proteins. Thermal analysis of methylated lysine variant hairpin peptides revealed an increase in thermal stability as the degree of methylation was increased, resulting in the most thermally stable beta-hairpin reported to date.

引用

页码：1525 / 1531

页数：7