生物物理过程在淀粉样蛋白聚集中的交叉成核作用及其在淀粉样蛋白病理学中的意义。
Biophysical processes underlying cross-seeding in amyloid aggregation and implications in amyloid pathology.
机构信息
Neurology, University of Michigan, Ann Arbor, MI 48109, USA; Biophysics, University of Michigan, Ann Arbor, MI 48109, USA.
Research Center for Bioconvergence Analysis, Korea Basic Science Institute, Ochang, Chungbuk 28119, South Korea.
出版信息
Biophys Chem. 2021 Feb;269:106507. doi: 10.1016/j.bpc.2020.106507. Epub 2020 Nov 19.
Abnormal aggregation of proteins into filamentous aggregates commonly associates with many diseases, such as Alzheimer's disease, Parkinson's disease and type-2 diabetes. These filamentous aggregates, also known as amyloids, can propagate their abnormal structures to either the same precursor molecules (seeding) or other protein monomers (cross-seeding). Cross-seeding has been implicated in the abnormal protein aggregation and has been found to facilitate the formation of physiological amyloids. It has risen to be an exciting area of research with a high volume of published reports. In this review article, we focus on the biophysical processes underlying the cross-seeding for some of the most commonly studied amyloid proteins. Here we will discuss the relevant literature related to cross-seeded polymerization of amyloid-beta, human islet amyloid polypeptide (hIAPP, or also known as amylin) and alpha-synuclein. SEVI (semen-derived enhancer of viral infection) amyloid formation by the cross-seeding between the bacterial curli protein and PAP is also briefly discussed.
蛋白质异常聚集形成纤维状聚集体通常与许多疾病有关，如阿尔茨海默病、帕金森病和 2 型糖尿病。这些纤维状聚集体，也称为淀粉样蛋白，可以将其异常结构传播到相同的前体分子（引发）或其他蛋白质单体（交叉引发）。交叉引发与异常蛋白质聚集有关，并已被发现有助于生理淀粉样蛋白的形成。它已成为一个令人兴奋的研究领域，发表了大量的报告。在这篇综述文章中，我们专注于一些研究最广泛的淀粉样蛋白的交叉引发的生物物理过程。在这里，我们将讨论与淀粉样蛋白-β、人胰岛淀粉样多肽（hIAPP，也称为胰岛淀粉样多肽）和α-突触核蛋白的交叉引发聚合相关的文献。细菌卷曲蛋白和 PAP 之间的交叉引发导致 SEVI（精液衍生的病毒感染增强子）淀粉样蛋白形成也被简要讨论。
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