Liang Fu-Cheng, Chen Rita P-Y, Lin Chun-Cheng, Huang Kuo-Ting, Chan Sunney I
Institute of Chemistry, Academia Sinica, Taipei, Taiwan, ROC.
Biochem Biophys Res Commun. 2006 Apr 7;342(2):482-8. doi: 10.1016/j.bbrc.2006.01.168. Epub 2006 Feb 9.
We have deployed the alpha-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.
我们已经部署了α-螺旋发夹肽（α-螺旋/转角/α-螺旋），并将其用作模型系统来探索糖基化和磷酸化如何影响肽的构象性质。通过核磁共振光谱法将缓冲溶液中修饰肽的天然构象与野生型肽的构象进行了比较。圆二色光谱法用于探测O-连接的β- N-乙酰葡糖胺和磷酸基团对肽整体折叠稳定性的影响。最后，使用纤维形成速率来推断这些化学修饰对α-向β-转变以及淀粉样蛋白形成的成核速率的影响。
