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• W2055941737 abstract "Toxic fibrillar aggregates of Islet Amyloid PolyPeptide (IAPP) appear as the physical outcome of a peptidic phase-transition signaling the onset of type-2 diabetes mellitus in different mammalian species. In particular, experimentally verified mutations on the amyloidogenic segment 20-29 in humans, cats and rats are highly correlated with the molecular aggregation propensities. Through a microcanonical analysis of the aggregation of IAPP_{20-29} isoforms, we show that a minimalist one-bead hydrophobic-polar continuum model for protein interactions properly quantifies those propensities from free-energy barriers. Our results highlight the central role of sequence-dependent hydrophobic mutations on hot spots for stabilization, and so for the engineering, of such biological peptides." @default.
• W2055941737 created "2016-06-24" @default.
• W2055941737 creator A5076277626 @default.
• W2055941737 date "2014-11-17" @default.
• W2055941737 modified "2023-10-06" @default.
• W2055941737 title "Breakout character of islet amyloid polypeptide hydrophobic mutations at the onset of type-2 diabetes" @default.
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• W2055941737 doi "https://doi.org/10.1103/physreve.90.052716" @default.
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• W2055941737 hasPublicationYear "2014" @default.
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