Tuning the conformation properties of a peptide by glycosylation and phosphorylation
Tuning the conformation properties of a peptide by glycosylation and phosphorylation
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DOI：
10.1016/j.bbrc.2006.01.168
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发表时间：
2006-04-07
影响因子：
3.1
通讯作者：
Chan, SI
中科院分区：
文献类型：
--
作者：
Liang, FC;Chen, RPY;Chan, SI
我们部署了α-螺旋发夹多肽(α-螺旋/TURN/α-螺旋)，并将其作为模型系统来探索糖基化和磷酸化如何影响多肽的构象性质。用核磁共振波谱对修饰后的多肽在缓冲溶液中的天然构象与野生型多肽的构象进行了比较。用圆二色谱研究了O-连接的β-GlcNAc和磷酸基团对多肽整体折叠稳定性的影响。最后，纤维形成的速度被用来推断这些化学修饰对α-β转变以及淀粉样蛋白形成的成核率的影响。(C)2006 Elsevier Inc.保留所有权利。
We have deployed the a-helical hairpin peptide (alpha-helix/turn/alpha-helix) and used it as a model system to explore how glycosylation and phosphorylation might affect the conformational properties of the peptide. The native conformations of the modified peptides in buffer solution have been compared with that of the wild-type peptide by nuclear magnetic resonance spectroscopy. Circular dichroism spectroscopy was used to probe the effects of an O-linked beta-GlcNAc and a phosphate group on the overall folding stability of the peptide. Finally, the rate of fibrillogenesis was used to infer the effects of these chemical modifications on the alpha-to-beta transition as well as the rate of nucleation of amyloidogenesis. (c) 2006 Elsevier Inc. All rights reserved.