从头设计的α-螺旋卷曲螺旋肽的多种糖基化。

Multiple glycosylation of de novo designed alpha-helical coiled coil peptides.

机构信息

Institute of Chemistry and Biochemistry, Organic Chemistry, Freie Universität Berlin, 14195 Berlin, Germany.

出版信息

Bioorg Med Chem. 2010 Jun 1;18(11):3703-6. doi: 10.1016/j.bmc.2010.03.061. Epub 2010 Mar 27.

DOI:10.1016/j.bmc.2010.03.061

PMID:20513637

Abstract

The aim of this study was to investigate the influence of multiple O-glycosylation in alpha-helical coiled coil peptides on the folding and stability. For this purpose we systematically incorporated one to six beta-galactose residues into the solvent exposed positions of a 26 amino acid long coiled coil helix. Surprisingly, circular dichroism spectroscopy showed no unfolding of the coiled coil structure for all glycopeptides. Thermally induced denaturations reveal a successive but relative low destabilization of the coiled coil structure upon introduction of beta-galactose residues. These first results indicate that O-glycosylation of the glycosylated variants is easily tolerated by this structural motif and pave the way for further functional studies.

摘要

本研究旨在探讨α-螺旋卷曲螺旋肽中多个 O-糖基化对其折叠和稳定性的影响。为此，我们系统地将一个到六个β-半乳糖基引入到 26 个氨基酸长的卷曲螺旋的溶剂暴露位置。令人惊讶的是，圆二色性光谱显示所有糖肽的卷曲螺旋结构都没有展开。热诱导变性表明，在引入β-半乳糖基后，卷曲螺旋结构会逐渐但相对较低地失稳。这些初步结果表明，该结构基序容易耐受糖基化变体的 O-糖基化，并为进一步的功能研究铺平了道路。