A Condensation-Ordering Mechanism in Nanoparticle-Catalyzed Peptide Aggregation

Abstract

Nanoparticles introduced in living cells are capable of strongly promoting the aggregation of peptides and proteins. We use here molecular dynamics simulations to characterise in detail the process by which nanoparticle surfaces catalyse the self- assembly of peptides into fibrillar structures. The simulation of a system of hundreds of peptides over the millisecond timescale enables us to show that the mechanism of aggregation involves a first phase in which small structurally disordered oligomers assemble onto the nanoparticle and a second phase in which they evolve into highly ordered beta-sheets as their size increases.

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• Direct observation of silver nanoparticle-ubiquitin corona formation
• Nucleation of amyloid fibrils
• Influence of Nanoparticle Size and Shape on Oligomer Formation of an Amyloidogenic Peptide
• Fibril elongation mechanisms of HET-s prion-forming domain: Topological evidence for growth polarity
• A Two-Step Biopolymer Nucleation Model Shows a Nonequilibrium Critical Point
• Hydrogen bond models for the simulation of protein folding and aggregation