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• W2136035568 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 and presence of copolymeric nanoparticles with different hydrophobic characters. For mutants with a high intrinsic stability and low intrinsic aggregation rate, we find that amyloid fibril formation is accelerated by nanoparticles. For mutants with a low intrinsic stability and high intrinsic aggregation rate, we find the opposite—a retardation of amyloid fibril formation by nanoparticles. Moreover, both catalytic and inhibitory effects are most pronounced with the least hydrophobic nanoparticles, which have a larger surface accessibility of hydrogen-bonding groups in the polymer backbone." @default.
• W2136035568 created "2016-06-24" @default.
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• W2136035568 creator A5070625264 @default.
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• W2136035568 date "2012-01-11" @default.
• W2136035568 modified "2023-09-30" @default.
• W2136035568 title "The Effect of Nanoparticles on Amyloid Aggregation Depends on the Protein Stability and Intrinsic Aggregation Rate" @default.
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• W2136035568 doi "https://doi.org/10.1021/la203078w" @default.
• W2136035568 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3265146" @default.
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• W2136035568 hasPublicationYear "2012" @default.
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