Looking for a Robust, Synthetic, Fully-Extended (2.05-Helical) Peptide Structure - Effect of Terminal Groups
作者:Fernando Formaggio、Marco Crisma、Cristina Peggion、Alessandro Moretto、Mariano Venanzi、Claudio Toniolo
DOI:10.1002/ejoc.201101273
日期:2012.1
The incorporation of α-amino acids with a quaternary α-carbon atom into a peptide provides a tool to effectively restrict the available range of its backbone conformations. Specifically, under favorable conditions, Cα,α-diethylglycine (Deg) homopeptides are known to preferentially adopt the fullyextended (2.05-helical) structure, which is characterized by the longest possible separation between two
将具有四元 α-碳原子的 α-氨基酸掺入肽中提供了一种有效限制其骨架构象可用范围的工具。具体而言,在有利条件下,已知 Cα, α-二乙基甘氨酸 (Deg) 同肽优先采用完全延伸(2.05-螺旋)结构,其特征在于两个相邻的 α-氨基酸 Cα 原子之间可能的最长间隔。我们研究了 N 和/或 C 端保护(或封闭)基团的性质对合成 Deg 同源肽系列中完全延伸构象与竞争性、较短 310 螺旋结构的相对稳定性的影响.