Conformationally restricted short peptides inhibit human islet amyloid polypeptide (hIAPP) fibrillization

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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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Islet amyloid polypeptide, islet amyloid, and diabetes mellitus.

Islet amyloid polypeptide (IAPP, or amylin) is one of the major secretory products of β-cells of the pancreatic islets of Langerhans. It is a regulatory peptide with putative function both locally in the islets, where it inhibits insulin and glucagon secretion, and at distant targets. It has binding sites in the brain, possibly contributing also to satiety regulation and inhibits gastric emptyi...

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Binuclear ruthenium complexes inhibit the fibril formation of human islet amyloid polypeptide

The deposition of human islet amyloid polypeptide (hIAPP) is closely correlated with type II diabetesmellitus (T2DM). hIAPPmisfolding, as a significant causative factor of T2DM, can lead to the failure of islet transplant. Therefore, preventing the aggregation of hIAPP is one of the most vital factors to treat T2DM. Mononuclear Ru complexes have recently been proved to inhibit the aggregation o...

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Adsorption and Orientation of Human Islet Amyloid Polypeptide (hIAPP) Monomer at Anionic Lipid Bilayers: Implications for Membrane-Mediated Aggregation

Protein misfolding and aggregation cause serious degenerative diseases, such as Alzheimer's and type II diabetes. Human islet amyloid polypeptide (hIAPP) is the major component of amyloid deposits found in the pancreas of type II diabetic patients. Increasing evidence suggests that β-cell death is related to the interaction of hIAPP with the cellular membrane, which accelerates peptide aggregat...

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ژورنال

عنوان ژورنال: Chemical Communications

سال: 2013

ISSN: 1359-7345,1364-548X

DOI: 10.1039/c3cc38982k