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• W2625492010 endingPage "909" @default.
• W2625492010 startingPage "899" @default.
• W2625492010 abstract "Accumulation of amyloid beta (A $$beta $$ ) peptide in the brain is responsible for debilitating neurodegenerative disease, namely, Alzheimer’s disease. We have carried out atomistic molecular dynamics simulation to study the early stages of the aggregation process of five full-length A $$beta $$ $$_{42}$$ peptide monomers with varying secondary structural contents in aqueous solution. Attempts have been made to study the conformational modifications of the A $$beta $$ peptide monomers and their dynamical features during the oligomer formation. In particular, specific molecular interactions that drive the association process leading to the formation of the stable oligomer have been identified. The calculations revealed that the helix–helix linkage plays an important role for bringing the unstructured regions of the monomers closer for self-assembly. Importantly, it is demonstrated that the contribution originating from the nonpolar interactions between the peptides and the corresponding nonpolar solvation more than compensates the weakening effect of unfavorable inter-peptide electrostatic interactions, thereby stabilizing the nucleated oligomer. Molecular dynamics simulations were performed to probe the early stages of aggregation of A $$beta $$ $$_{42}$$ peptides. The calculations revealed that the helix–helix linkage plays an important role for bringing the unstructured regions of the monomers closer for self-assembly. Further, the nucleated oligomer was found to be stabilized primarily by nonpolar inter-peptide interactions." @default.
• W2625492010 created "2017-06-23" @default.
• W2625492010 creator A5048994371 @default.
• W2625492010 creator A5051434187 @default.
• W2625492010 date "2017-06-15" @default.
• W2625492010 modified "2023-09-27" @default.
• W2625492010 title "In silico studies of the early stages of aggregation of A $$beta _{42}$$ β 42 peptides" @default.
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• W2625492010 doi "https://doi.org/10.1007/s12039-017-1306-2" @default.
• W2625492010 hasPublicationYear "2017" @default.
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