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Disclosing the Interaction of Gold Nanoparticles with A?(1-40) Monomers through Replica Exchange Molecular Dynamics Simulations.

ABSTRACT: Amyloid-? aggregation is one of the principal causes of amyloidogenic diseases that lead to the loss of neuronal cells and to cognitive impairments. The use of gold nanoparticles treating amyloidogenic diseases is a promising approach, because the chemistry of the gold surface can be tuned in order to have a specific binding, obtaining effective tools to control the aggregation. In this paper, we show, by means of Replica Exchange Solute Tempering Molecular Simulations, how electrostatic interactions drive the absorption of Amyloid-? monomers onto citrates-capped gold nanoparticles. Importantly, upon binding, amyloid monomers show a reduced propensity in forming ?-sheets secondary structures that are characteristics of mature amyloid fibrils.

SUBMITTER: Tavanti F

PROVIDER: S-EPMC7792802 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature

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Disclosing the Interaction of Gold Nanoparticles with Aβ(1-40) Monomers through Replica Exchange Molecular Dynamics Simulations.

Tavanti Francesco F Pedone Alfonso A Menziani Maria Cristina MC

International journal of molecular sciences 20201222 1

Amyloid-β aggregation is one of the principal causes of amyloidogenic diseases that lead to the loss of neuronal cells and to cognitive impairments. The use of gold nanoparticles treating amyloidogenic diseases is a promising approach, because the chemistry of the gold surface can be tuned in order to have a specific binding, obtaining effective tools to control the aggregation. In this paper, we show, by means of Replica Exchange Solute Tempering Molecular Simulations, how electrostatic interac ...[more]

PMID: 33375086

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