The assembly of amyloidogenic peptides and proteins, such as the β-amyloid peptide, α-synuclein, huntingtin, tau, and islet amyloid polypeptide, into amyloid fibrils and oligomers is directly linked to amyloid diseases, such as Alzheimer's, Parkinson's, and Huntington's diseases, frontotemporal dementias, and type II diabetes. Although amyloid oligomers have emerged as especially important in amyloid diseases, high-resolution structures of the oligomers formed by full-length amyloidogenic peptides and proteins have remained elusive. Investigations of oligomers assembled from fragments or stabilized β-hairpin segments of amyloidogenic peptides and proteins have allowed investigators to illuminate some of the structural, biophysical, and biological properties of amyloid oligomers. Here, we summarize recent advances in the application of these peptide model systems to investigate and understand the structures, biological properties, and biophysical properties of amyloid oligomers.

中文翻译：

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用肽模型系统探索淀粉样蛋白寡聚体。

淀粉样肽和蛋白质（例如 β-淀粉样肽、α-突触核蛋白、亨廷顿蛋白、tau 和胰岛淀粉样多肽）组装成淀粉样蛋白原纤维和寡聚体与淀粉样蛋白疾病（例如阿尔茨海默病、帕金森病和亨廷顿病）直接相关、额颞叶痴呆和II型糖尿病。尽管淀粉样蛋白寡聚体在淀粉样蛋白疾病中显得尤为重要，但由全长淀粉样肽和蛋白质形成的寡聚体的高分辨率结构仍然难以捉摸。对由淀粉样肽和蛋白质的片段或稳定的 β-发夹片段组装的寡聚体的研究使研究人员能够阐明淀粉样蛋白寡聚体的一些结构、生物物理和生物学特性。这里，