将α-氨基异丁酸引入寡聚缬氨酸序列所引起的螺旋诱导程度。
Extent of Helical Induction Caused by Introducing α-Aminoisobutyric Acid into an Oligovaline Sequence.
作者信息
Tsuji Genichiro, Misawa Takashi, Doi Mitsunobu, Demizu Yosuke
机构信息
Division of Organic Chemistry, National Institute of Health Sciences, Kanagawa 210-9501, Japan.
Osaka University of Pharmaceutical Sciences, Osaka 569-1094, Japan.
出版信息
ACS Omega. 2018 Jun 14;3(6):6395-6399. doi: 10.1021/acsomega.8b01030. eCollection 2018 Jun 30.
The preferred conformations of a dodecapeptide composed of l-valine (l-Val) and α-aminoisobutyric acid (Aib) residues, Boc-(l-Val-l-Val-Aib)-OMe (), were analyzed in solution and in the crystalline state. Peptide predominantly folded into a mixture of α- and 3-() helical structures in solution and a () α helix in the crystalline state.
对由L-缬氨酸（L-Val）和α-氨基异丁酸（Aib）残基组成的十二肽Boc-(L-Val-L-Val-Aib)-OMe（ ）在溶液和晶体状态下的优选构象进行了分析。该肽在溶液中主要折叠成α-螺旋和3-（ ）螺旋结构的混合物，在晶体状态下为（ ）α螺旋。
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