Does deamidation of islet amyloid polypeptide accelerate amyloid fibril formation?
Does deamidation of islet amyloid polypeptide accelerate amyloid fibril formation?
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DOI：
10.1039/c8cc06675b
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发表时间：
2018-12-21
影响因子：
4.9
通讯作者：
O'Connor, Peter B.
中科院分区：
文献类型：
--
作者：
Lam, Yuko P. Y.;Wootton, Christopher A.;O'Connor, Peter B.
质谱法已用于确定脱酰胺位点和脱酰胺人胰岛淀粉样蛋白多肽（hIAPP）的聚集区域。在可能的脱酰胺位点具有异天冬氨酸残基突变的突变体 hIAPP 显示出非常不同的原纤维形成行为，这与观察到的脱酰胺诱导的 hIAPP 聚集加速相关。
Mass spectrometry has been applied to determine the deamidation sites and the aggregation region of the deamidated human islet amyloid polypeptide (hIAPP). Mutant hIAPP with iso-aspartic residue mutations at possible deamidation sites showed very different fibril formation behaviour, which correlates with the observed deamidation-induced acceleration of hIAPP aggregation.