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• W3136399692 abstract "The Human islet amyloid polypeptide (h-IAPP, also known as Amylin) is a peptide hormone which is co-packaged and co-secreted with insulin by the pancreatic beta-cells. In its normal physiological role, it is associated with glucose homeostasis, control of gastric emptying, suppression of glucagon release and satiety regulation. The secreted amylin has the propensity to form membrane permit toxic oligomers which causes it to aggregate into dense insoluble fibrillar deposits (amyloid deposits) that accumulate in the pancreas. Deposits has been postulated to be one of the main contributors to impaired insulin secretion and pancreatic β-cell death in approximately 90% of type 2 diabetic (T2DM) patients and eventually lead to cell dysfunction and apoptosis. Some of the factors that cause aggregation include- development of metabolic stress, genetic mutations of IAPP, and aberrations in IAPP processing, interaction with metal ions and environmental conditions of the cell. Hence current Insilico study focuses towards understanding the mechanism for aggregation of the peptide-metal complex and identification of novel compounds that prevent cytotoxic polypeptide self-assembly and amyloidogenesis.Our initial analysis involved extensive sequence, structure and mutational analysis of IAPP and 1–37 peptides via Insilco sequence alignment between mutants and wild-type. Several point mutations were studied and compared among different species; our results revealed interesting differences between human, rat, mouse, cat, monkey, dog etc. The effect of 15 single-point mutations like A13E, F15I, F15L, L16Q, S20K, S20G, N22L, F23P, G24P, A25D, A25P, L27P, L27G, S28P, Y37L were also recognized within the human amylin sequence. Similarly, outcomes elucidate that the S20G and S20K mutations may lead to faster amyloid formation and amyloidogenesis. Mutations from SER (S28P), ALA (A25P) to PRO Inhibits Amyloid Aggregation. Docking analysis of metals like Al, Cu and Zn with amylin showed strong binding free energy for interaction with H18 and the C-terminal residues, Ser19, Ser20, and Asn22, which are key to β-sheet formation and this could promote fibrillation and aggregation of hIAPP. Whereas, screened natural compounds and small molecules docked interact across hydrophobic residues Phe-Gly-Ala (23–25). Thus, our study offers understanding of the role of metal ions in the aggregation/inhibitory effect on amylin peptides and screened small molecules provides a computational framework for the future design of anti-amyloid aggregation across T2DM." @default.
• W3136399692 created "2021-03-29" @default.
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• W3136399692 date "2020-01-08" @default.
• W3136399692 modified "2023-09-23" @default.
• W3136399692 title "In-Silico Studies on Human Islet Amyloid Polypeptide (H-Iapp) Aggregation Studies With Metal Ion Interactions and Design for Anti-Amyloid Aggregation Molecules Implicated in Type 2 Diabetes Mellitus." @default.
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