Department of Chemistry, University of Michigan, Ann Arbor, MI, USA.
Chem Commun (Camb). 2020 Nov 7;56(86):13129-13132. doi: 10.1039/d0cc04803h. Epub 2020 Oct 2.
In this study, the effect of CurDAc, a water-soluble curcumin derivative, on the formation and stability of amyloid fibers is revealed. CurDAc interaction with amyloid is structurally selective, which is reflected in a strong interference with hIAPP aggregation while showing weaker interactions with human-calcitonin and amyloid-β in comparison. Remarkably, CurDAc also exhibited potent fiber disaggregation for hIAPP generating a toxic oligomeric species.
在这项研究中，揭示了水溶性姜黄素衍生物 CurDAc 对淀粉样纤维的形成和稳定性的影响。CurDAc 与淀粉样物的相互作用具有结构选择性，这反映在强烈干扰 hIAPP 聚集的同时，与人类降钙素和淀粉样-β的相互作用较弱。值得注意的是，CurDAc 还表现出对 hIAPP 的强大纤维解聚作用，生成有毒的寡聚体。
