The aggregation of the 37‐amino acid polypeptide human islet amyloid polypeptide (hIAPP), as either insoluble amyloid or as small oligomers, appears to play a direct role in the death of human pancreatic β‐islet cells in type 2 diabetes. hIAPP is considered to be one of the most amyloidogenic proteins known. The quick aggregation of hIAPP leads to the formation of toxic species, such as oligomers and fibers, that damage mammalian cells (both human and rat pancreatic cells). Whether this toxicity is necessary for the progression of type 2 diabetes or merely a side effect of the disease remains unclear. If hIAPP aggregation into toxic amyloid is on‐path for developing type 2 diabetes in humans, islet amyloid polypeptide (IAPP) aggregation would likely need to play a similar role within other organisms known to develop the disease. In this work, we compared the aggregation potential and cellular toxicity of full‐length IAPP from several diabetic and nondiabetic organisms whose aggregation propensities had not yet been determined for full‐length IAPP.

中文翻译：

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天然存在的全长动物IAPP变体的淀粉样变性。

37个氨基酸的多肽人类胰岛淀粉样多肽（hIAPP）的聚集体，无论是不溶性淀粉样蛋白还是小的寡聚体，似乎在2型糖尿病的人类胰岛β胰岛细胞死亡中起着直接作用。hIAPP被认为是已知的最具淀粉样蛋白的蛋白质之一。hIAPP的快速聚集导致形成有毒物质，例如寡聚体和纤维，从而破坏哺乳动物细胞（人和大鼠的胰腺细胞）。这种毒性对于2型糖尿病的进展是必需的还是仅是疾病的副作用尚不清楚。如果hIAPP聚集为有毒的淀粉样蛋白正在人类中发展为2型糖尿病，那么胰岛淀粉样多肽（IAPP）聚集可能需要在已知会导致该疾病的其他生物体内发挥相似的作用。在这项工作中