Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto, Japan.
FEBS Lett. 2011 Apr 6;585(7):1097-102. doi: 10.1016/j.febslet.2011.03.014. Epub 2011 Mar 12.
A detailed analysis of the NMR spectra of amyloid-β (Aβ) peptide revealed a decrease in signal intensity at higher temperature, due to a reversible conformational change of the molecule. Although peak intensity did not depend on peptide concentrations, the intensity in the region from D23 to A30 depended significantly on temperature. During the early stages of Aβ aggregation, each molecule might adopt transiently a turn conformation at around D23-A30, which converts mutually with a random coil. Stabilization of a turn by further conformational change and/or molecular association would lead to the formation of a "nucleus" for amyloid fibrils.
对淀粉样蛋白-β（Aβ）肽的 NMR 谱进行了详细分析，结果表明，随着温度的升高，信号强度降低，这是由于分子的可逆构象变化所致。尽管峰强度与肽浓度无关，但 D23 到 A30 区域的强度与温度有显著的依赖性。在 Aβ聚集的早期阶段，每个分子可能在 D23-A30 处暂时采用一种转角构象，这种构象与无规卷曲之间可以相互转换。进一步的构象变化和/或分子缔合使转角稳定，从而形成淀粉样纤维的“核”。
