The effect of nanoparticles on amyloid aggregation depends on the protein stability and intrinsic aggregation rate.

ABSTRACT: Nanoparticles interfere with protein amyloid formation. Catalysis of the process may occur due to increased local protein concentration and nucleation on the nanoparticle surface, whereas tight binding or a large particle/protein surface area may lead to inhibition of protein aggregation. Here we show a clear correlation between the intrinsic protein stability and the nanoparticle effect on the aggregation rate. The results were reached for a series of five mutants of single-chain monellin differing in intrinsic stability toward denaturation, for which a correlation between protein stability and aggregation propensity has been previously documented by Szczepankiewicz et al. [Mol. Biosyst.20107 (2), 521-532]. The aggregation process was monitored by thioflavin T fluorescence in the absence

SUBMITTER: Cabaleiro-Lago C 

PROVIDER: S-EPMC3265146 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature