Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide.
نویسندگان
چکیده
The aggregation of human islet amyloid polypeptide (hIAPP) has been linked to beta-cell death in type II diabetes. Zinc present in secretory granules has been shown to affect this aggregation. A combination of EXAFS, NMR, and AFM experiments shows that the influence of zinc is most likely due to the stabilization of prefibrillar aggregates of hIAPP.
منابع مشابه
Formation of lamellar micelle-like oligomers and membrane disruption revealed by the study of short peptide hIAPP18-27.
Prefibrillar amyloid aggregates of proteins are known as cytotoxic species and a common pathogenic factor for many degenerative diseases. The mechanism underlying the formation and cytotoxicity of prefibrillar aggregates is believed to be independent of the actual nature of the amyloid protein. In this study, we monitored the formation of the peptide oligomers and examined the disruptive effect...
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Amylin, a small peptide co-secreted from pancreatic β-cells together with insulin, is one of the hallmarks of type II diabetes. In the course of this disease, it misfolds into small oligomers or into an aggregated β-sheet amyloid fiber. The misfolding mechanism is not yet well understood, but it is clear that metal ions such as zinc and copper play an important role in the process. In this work...
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ورودعنوان ژورنال:
- Chemical communications
دوره 49 32 شماره
صفحات -
تاریخ انتشار 2013