它是众所周知的聚集淀粉 --Cu2+ 导致的肽(A) 与孵化时间,答案 pH,和温度有关。在这个工作, A142 的聚集在不同孵化时间和温度面对在酸的条件下面的 Cu2+ 被学习(例如 25 和 37 ????? ?? 匠吗??
It is well known that the aggregation of amyloid-β peptide (Aβ) induced by Cu^2+ is related to incubation time, solu-tion pH, and temperature. In this work, the aggregation of Aβ1-42 in the presence of Cu^2+ under acidic conditions was studied at different incubation time and temperature (e.g. 25 and 37℃). Incubation temperature, pH, and the presence of Cu^2+ in Aβ solution were confirmed to alter the morphology of aggregation (fibrils or amorphous aggregates), and the morphology is pivotal for Aβ neuro-toxicity and AIzheimer disease (AD) development. The results of atomic force microscopy (AFM) indicated that the formation of Aβ fibrous morphology is preferred at lower pH, but Cu^2+ induced the formation of amorphous aggregates. The aggregation rate of Aβ was increased with the elevation of temperature. These results were further confirmed by fluorescence spectroscopy and circular di-chroism spectroscopy and it was found that the formation of β-sheet structure was inhibited by Cu^2+ binding to Aβ. The result was consistent with AFM observation and the fibrillation process was restrained. We believe that the local charge state in hydrophilic domain of Aβ may play a dom-inant role in the aggregate morphology due to the strong steric hindrance. This research will be valuable for under-standing of Aβ toxicity in AD.