Multiple glycosylation of de novo designed α-helical coiled coil peptides
Multiple glycosylation of de novo designed α-helical coiled coil peptides
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DOI：
10.1016/j.bmc.2010.03.061
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发表时间：
2010-06-01
影响因子：
3.5
通讯作者：
Koksch, Beate
中科院分区：
文献类型：
--
作者：
Falenski, Jessica A.;Gerling, Ulla I. M.;Koksch, Beate
本研究的目的是研究α-螺旋卷曲肽中的多个O-糖基化对折叠和稳定性的影响。为此，我们系统地将一到六个β-半乳糖残基掺入26个氨基酸长卷曲螺旋的溶剂暴露位置。令人惊讶的是，圆二色光谱显示所有糖肽的卷曲螺旋结构均未展开。热诱导变性揭示了引入β-半乳糖残基后卷曲螺旋结构连续但相对较低的不稳定。这些初步结果表明，糖基化变体的 O-糖基化很容易被该结构基序所耐受，并为进一步的功能研究铺平了道路。 (C) 2010 Elsevier Ltd. 保留所有权利。
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. (C) 2010 Elsevier Ltd. All rights reserved.