Riemen Alexander J, Waters Marcey L
Department of Chemistry, CB 3290, University of North Carolina, Chapel Hill, North Carolina 27599, USA.
Biochemistry. 2009 Feb 24;48(7):1525-31. doi: 10.1021/bi801706k.
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.
两个色氨酸残基被引入到β-发夹肽的一个面上,以形成一个芳香口袋,该口袋通过阳离子-π相互作用与赖氨酸或N-甲基化赖氨酸相互作用。发现这两个色氨酸残基与赖氨酸侧链堆积,形成了一个类似于在三甲基化赖氨酸受体蛋白中观察到的芳香口袋。对甲基化赖氨酸变体发夹肽的热分析表明,随着甲基化程度的增加,热稳定性增强,从而产生了迄今为止报道的最耐热的β-发夹。