Controlling the helical screw sense of peptides with C-terminal L-valine
Controlling the helical screw sense of peptides with C-terminal L-valine
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DOI：
10.1002/psc.1213
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发表时间：
2010-03-01
影响因子：
2.1
通讯作者：
Kurihara, Masaaki
中科院分区：
文献类型：
--
作者：
Demizu, Yosuke;Yamagata, Nanako;Kurihara, Masaaki
将一个手性L-缬氨酸（L-Val）插入由α-氨基异丁酸（Aib）和α，β-脱氢苯丙氨酸（Delta（z）Phe）残基构建的非手性肽段的C-末端位置。红外光谱、核磁共振氢谱和圆二色性谱表明，五肽Boc-Aib-Delta Phe-（Aib）（2）-L-Val-NH-Bn（3）和六肽Boc-Aib-Delta Phe-（Aib）（3）-L-Val-NH-Bn（4）在溶液中的主要构象均为右旋（P）3（10）螺旋结构。3和4的X射线晶体学分析表明，在它们的结晶状态下仅存在右旋（P）3（10）-螺旋结构。并通过分子力学计算对4的构象进行了研究。版权所有（C）2010欧洲肽协会和约翰威利父子有限公司。
One chiral L-valine (L-Val) was inserted into the C-terminal position of achiral peptide segments constructed from alpha-aminoisobutyric acid (Aib) and alpha,beta-dehydrophenylalanine (Delta(z)Phe) residues. The IR, (1)H NMR and CD spectra indicated that the dominant conformations of the pentapeptide Boc-Aib-Delta Phe-(Aib)(2)-L-Val-NH-Bn (3) and the hexapeptide Boc-Aib-Delta Phe-(Aib)(3)-L-Val-NH-Bn (4) in solution were both right-handed (P) 3(10)-helical structures. X-ray crystallographic analyses of 3 and 4 revealed that only a right-handed (P) 3(10)-helical structure was present in their crystalline states. The conformation of 4 was also studied by molecular-mechanics calculations. Copyright (C) 2010 European Peptide Society and John Wiley & Sons, Ltd.