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- W2164425022 endingPage "1304" @default.
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- W2164425022 abstract "We investigate the molecular mechanism of monomer addition to a growing amyloid fibril composed of the main amyloidogenic region from the insulin peptide hormone, the LVEALYL heptapeptide. Applying transition path sampling in combination with reaction coordinate analysis reveals that the transition from a docked peptide to a locked, fully incorporated peptide can occur in two ways. Both routes involve the formation of backbone hydrogen bonds between the three central amino acids of the attaching peptide and the fibril, as well as a reorientation of the central Glu side chain of the locking peptide toward the interface between two β-sheets forming the fibril. The mechanisms differ in the sequence of events. We also conclude that proper docking is important for correct alignment of the peptide with the fibril, as alternative pathways result in misfolding." @default.
- W2164425022 created "2016-06-24" @default.
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- W2164425022 date "2012-09-01" @default.
- W2164425022 modified "2023-09-29" @default.
- W2164425022 title "Elucidating the Locking Mechanism of Peptides onto Growing Amyloid Fibrils through Transition Path Sampling" @default.
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- W2164425022 doi "https://doi.org/10.1016/j.bpj.2012.07.056" @default.
- W2164425022 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3446680" @default.
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