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- W2052162433 startingPage "e47150" @default.
- W2052162433 abstract "The amyloid fibrils formed by islet amyloid polypeptide (IAPP) are associated with type II diabetes. One of the proposed mechanisms of the toxicity of IAPP is that it causes membrane damage. The fatal mutation of S20G human IAPP was reported to lead to early onset of type II diabetes and high tendency of amyloid formation in vitro. Characterizing the structural features of the S20G mutant in its monomeric state is experimentally difficult because of its unusually fast aggregation rate. Computational work complements experimental studies. We performed a series of molecular dynamics simulations of the monomeric state of human variants in the membrane. Our simulations are validated by extensive comparisons with experimental data. We find that a helical disruption at His18 is common to both human variants. An L-shaped motif of S20G mutant is observed in one of the conformational families. This motif that bends at His18 resembles the overall topology of IAPP fibrils. The conformational preorganization into the fibril-like topology provides a possible explanation for the fast aggregation rate of S20G IAPP." @default.
- W2052162433 created "2016-06-24" @default.
- W2052162433 creator A5032769652 @default.
- W2052162433 creator A5037437663 @default.
- W2052162433 creator A5043239673 @default.
- W2052162433 date "2012-11-02" @default.
- W2052162433 modified "2023-10-16" @default.
- W2052162433 title "Conformations of Islet Amyloid Polypeptide Monomers in a Membrane Environment: Implications for Fibril Formation" @default.
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- W2052162433 doi "https://doi.org/10.1371/journal.pone.0047150" @default.
- W2052162433 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3487734" @default.
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- W2052162433 hasPublicationYear "2012" @default.
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