C-糖基化β(2)-肽和β/β(2)-肽的制备及构象分析

Preparation and conformational analysis of C-glycosyl beta(2)- and beta/beta(2)-peptides.

作者信息

Inaba Yoko, Kawakami Toru, Aimoto Saburo, Ikegami Takahisa, Takeuchi Takae, Nakazawa Takashi, Yano Shigenobu, Mikata Yuji

机构信息

Department of Interdisciplinary Materials Science, Nara Women's University, Nara 630-8506, Japan.

出版信息

Carbohydr Res. 2009 Mar 31;344(5):613-26. doi: 10.1016/j.carres.2009.01.018. Epub 2009 Jan 23.

DOI:10.1016/j.carres.2009.01.018

PMID:19217080

Abstract

Ten C-glycosyl beta(2)- and beta/beta(2)-peptides with three to eight amino acid residues have been prepared. Solution and solid-phase peptide syntheses were employed to assemble beta(2)-amino acids in which C-glycosylic substituents are attached to the C-2 position of beta-amino acids. Conformational analysis of the C-glycosyl beta(2)-peptides using NMR and CD spectra indicates that the tripeptide can form a helical secondary structure. Besides, helix directions of the C-glycosyl beta/beta(2)-peptides are governed by the configuration at the alpha-carbon of the peptide backbone that originates from the stereocenter of the C-glycosyl beta(2)-amino acids.

摘要

已经制备了十种具有三到八个氨基酸残基的C-糖基化β(2)-肽和β/β(2)-肽。采用溶液和固相肽合成法来组装β(2)-氨基酸，其中C-糖基取代基连接到β-氨基酸的C-2位。使用核磁共振（NMR）和圆二色光谱（CD）对C-糖基化β(2)-肽进行构象分析表明，三肽可以形成螺旋二级结构。此外，C-糖基化β/β(2)-肽的螺旋方向由肽主链α-碳上的构型决定，该构型源自C-糖基化β(2)-氨基酸的立体中心。