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- W2072904503 abstract "Self-assembled forms of the 4 kDa amyloid beta (Aβ) peptide, itself formed from proteolytic cleavage of the membrane embedded precursor, is strongly implicated in the onset of the neurodegenerative Alzheimer's disease (AD). While amyloid aggregates found in patients' brains are predominantly composed of the peptide's fibrillar forms, its soluble oligomers have been reported to aggravate the peptide's neurotoxicity. It is recognized, however, that all self-assembly pathways arise from the peptide's initial nucleation, and therefore eliciting mechanistic details of this process as a function of physico-chemical conditions could unearth valuable strategies for disrupting the peptide's neurotoxicity. With atomistic molecular dynamics simulations, we have shown very recently that the full-length peptide undergoes enthalpy-driven adsorption on the hydrophobic surface of high curvature (Biophys. J. 2012, 102, 1889; Phys. Chem. Chem. Phys. 2013, 15, 837). The process, initiated by the peptide's central hydrophobic core (L17VFFA21), is comprised of a dewetting transition followed by π-π stacking interactions with the surface. We report here the effect of the hydrophobic surface on the initial dimerization process of the full-length Aβ. While the interactions with the surface cannot out compete the strong monomer-monomer interactions, they are capable to a large extent in destabilizing pre-formed Aβ dimers. We further performed adaptive biasing force based free energy calculations to compare the Aβ trimerization process arising from addition of a monomeric unit to the surface adsorbed, weakened dimer complex, to that in pure solution. Our results indicate that presence of hydrophobic surfaces is likely to weaken the initial nucleation processes, and could eventually slow the self-assembly kinetics. These results should be of significance in the design of therapeutics aimed at countering the neurotoxic effects of Aβ oligomers." @default.
- W2072904503 created "2016-06-24" @default.
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- W2072904503 date "2014-01-01" @default.
- W2072904503 modified "2023-09-30" @default.
- W2072904503 title "Atomistic Simulations Lend Mechanistic Insights into Plausible Ways of Perturbing the Nucleation Thermodynamics of the Full-Length Aβ Peptide" @default.
- W2072904503 doi "https://doi.org/10.1016/j.bpj.2013.11.3782" @default.
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