Structure of peptide inhibitor of human islet amyloid polypeptide fibrillization
نویسندگان
چکیده
منابع مشابه
Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization†
Type 2 Diabetes Mellitus (T2DM) is one of the most prevalent endocrine disorders underlining the importance of developingmolecular therapies to mitigate T2DM. It is characterized by a significant decrease in b-cell mass, insulin resistance and presence of amyloid plaques in which human islet amyloid polypeptide (hIAPP) is the major protein component. hIAPP is a 37-residue polypeptide co-secrete...
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The hormone islet amyloid polypeptide (IAPP, or amylin) plays a role in glucose homeostasis but aggregates to form islet amyloid in type-2 diabetes. Islet amyloid formation contributes to β-cell dysfunction and death in the disease and to the failure of islet transplants. Recent work suggests a role for IAPP aggregation in cardiovascular complications of type-2 diabetes and hints at a possible ...
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Assembly of amyloid-beta peptide (Aβ) into cytotoxic oligomeric and fibrillar aggregates is believed to be a major pathologic event in Alzheimer's disease (AD) and interfering with Aβ aggregation is an important strategy in the development of novel therapeutic approaches. Prior studies have shown that the double N-methylated analogue of islet amyloid polypeptide (IAPP) IAPP-GI, which is a confo...
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متن کاملZinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide.
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.
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ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations of Crystallography
سال: 2011
ISSN: 0108-7673
DOI: 10.1107/s0108767311092798