期刊
CHEMISTRY AND PHYSICS OF LIPIDS
卷 234, 期 -, 页码 -出版社
ELSEVIER IRELAND LTD
DOI: 10.1016/j.chemphyslip.2020.105010
关键词
Islet amyloid polypeptide (IAPP); Amyloid aggregation; Oligomers; Biomembranes; Mitochondria; Anti-amyloid compounds
资金
- Research, Innovation & Development Trust (RIDT) of the University of Malta [El 6L062-01]
- Faculty of Medicine and Surgery, University of Malta [MDSBM20-24]
- Tertiary Education Scholarship Scheme (TESS) of the Ministry for Education and Employment, Malta
hIAPP is a peptide hormone associated with protein misfolding disorders, impacting soluble amyloid deposition in the pancreas and brain through interaction with biological membranes. Future research should involve more physiologically-relevant studies for a better understanding of in vivo interactions, and there is an urgent need for developing effective therapeutic strategies to inhibit hIAPP-phospholipid interactions.
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.
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