Toniolo C, Crisma M, Formaggio F, Valle G, Cavicchioni G, Precigoux G, Aubry A, Kamphuis J
Department of Organic Chemistry, University of Padova, Italy.
Biopolymers. 1993 Jul;33(7):1061-72. doi: 10.1002/bip.360330708.
The structural preferences of peptides (and depsipeptides) from the achiral MeAib and Hib residues, and the chiral Iva, (alpha Me) Val, (alpha Me) Leu, and (alpha Me) Phe residues, as determined by conformational energy computations, x-ray diffraction analyses, and 1H-nmr and spectroscopic studies, are reviewed and compared with literature data on Aib-containing peptides. The results obtained indicate that helical structures are preferentially adopted by peptides rich in these alpha-amino acids methylated at the alpha-carbon. Intriguing experimental findings on the impact of the chirality of Iva, (alpha Me) Val, and (alpha Me) Phe residues on helix screw sense are illustrated.
通过构象能量计算、X射线衍射分析以及1H-核磁共振和光谱研究，确定了来自非手性的甲基丙氨酸（MeAib）和高丝氨酸（Hib）残基，以及手性的异缬氨酸（Iva）、α-甲基缬氨酸（αMe）Val、α-甲基亮氨酸（αMe）Leu和α-甲基苯丙氨酸（αMe）Phe残基的肽（和缩肽）的结构偏好，并与含Aib肽的文献数据进行了比较。所得结果表明，富含这些在α-碳上甲基化的α-氨基酸的肽优先采用螺旋结构。文中阐述了关于Iva、αMe Val和αMe Phe残基的手性对螺旋旋向影响的有趣实验发现。
