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• W2058902745 startingPage "e58297" @default.
• W2058902745 abstract "Background Protein aggregation is linked to the onset of an increasing number of human nonneuropathic (either localized or systemic) and neurodegenerative disorders. In particular, misfolding of native α-helical structures and their self-assembly into nonnative intermolecular β-sheets has been proposed to trigger amyloid fibril formation in Alzheimer’s and Parkinson’s diseases. Methods Here, we use a battery of biophysical techniques to elucidate the conformational conversion of native α-helices into amyloid fibrils using an all-α FF domain as a model system. Results We show that under mild denaturing conditions at low pH this FF domain self-assembles into amyloid fibrils. Theoretical and experimental dissection of the secondary structure elements in this domain indicates that the helix 1 at the N-terminus has both the highest α-helical and amyloid propensities, controlling the transition between soluble and aggregated states of the protein. Conclusions The data illustrates the overlap between the propensity to form native α-helices and amyloid structures in protein segments. Significance The results presented contribute to explain why proteins cannot avoid the presence of aggregation-prone regions and indeed use stable α-helices as a strategy to neutralize such potentially deleterious stretches." @default.
• W2058902745 created "2016-06-24" @default.
• W2058902745 creator A5024123974 @default.
• W2058902745 creator A5025858582 @default.
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• W2058902745 date "2013-03-07" @default.
• W2058902745 modified "2023-10-16" @default.
• W2058902745 title "The N-terminal Helix Controls the Transition between the Soluble and Amyloid States of an FF Domain" @default.
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• W2058902745 doi "https://doi.org/10.1371/journal.pone.0058297" @default.
• W2058902745 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3591442" @default.
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