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- W3103271710 endingPage "105010" @default.
- W3103271710 startingPage "105010" @default.
- W3103271710 abstract "Human islet amyloid polypeptide (hIAPP), otherwise known as amylin, is a 37-residue peptide hormone which is reported to be a common factor in protein misfolding disorders such as type-2 diabetes mellitus, Alzheimer’s disease and Parkinson’s disease, due to deposition of insoluble hIAPP amyloid in the pancreas and brain. Multiple studies point to the importance of the peptide’s interaction with biological membranes and the cytotoxicity of hIAPP species. Here, we discuss the aggregation pathways of hIAPP amyloid fibril formation and focus on the complex interplay between membrane-mediated assembly of hIAPP and the associated mechanisms of membrane damage caused by the peptide species. Mitochondrial membranes, which are unique in their lipid composition, are proposed as prime targets for the early intracellular formation of hIAPP toxic entities. We suggest that future studies should include more physiologically-relevant and in-cell studies to allow a more accurate model of in vivo interactions. Finally, we underscore an urgent need for developing effective therapeutic strategies aimed at hindering hIAPP-phospholipid interactions." @default.
- W3103271710 created "2020-11-23" @default.
- W3103271710 creator A5013995244 @default.
- W3103271710 creator A5081825356 @default.
- W3103271710 creator A5082332849 @default.
- W3103271710 date "2021-01-01" @default.
- W3103271710 modified "2023-09-27" @default.
- W3103271710 title "The human islet amyloid polypeptide in protein misfolding disorders: Mechanisms of aggregation and interaction with biomembranes" @default.
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