The Amyloid Formation Mechanism in Human IAPP: Dimers Have β-Strand Monomer−Monomer Interfaces
نویسندگان
چکیده
منابع مشابه
Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet.
Amyloid formation is implicated in more than 20 human diseases, yet the mechanism by which fibrils form is not well understood. We use 2D infrared spectroscopy and isotope labeling to monitor the kinetics of fibril formation by human islet amyloid polypeptide (hIAPP or amylin) that is associated with type 2 diabetes. We find that an oligomeric intermediate forms during the lag phase with parall...
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Islet amyloid polypeptide (IAPP or amylin) forms amyloid deposits in the islets of Langerhans; a process that is believed to contribute to the progression of type 2 diabetes and to the failure of islet transplants. An emerging theme in amyloid research is the hypothesis that the toxic species produced during amyloid formation by different polypeptides share common features and exert their effec...
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ژورنال
عنوان ژورنال: Journal of the American Chemical Society
سال: 2011
ISSN: 0002-7863,1520-5126
DOI: 10.1021/ja1081537