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The effect of nanoparticles on amyloid aggregation depends on the protein stability and intrinsic aggregation rate.
Lunds universitet.ORCID iD: 0000-0002-3200-9945
Lunds universitet.
Lunds universitet.
2012 (English)In: Langmuir, ISSN 0743-7463, E-ISSN 1520-5827, Vol. 28, no 3, p. 1852-1857Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2012. Vol. 28, no 3, p. 1852-1857
Keywords [en]
Solid-liquid interfaces, Alpha-B-Crystallin, Fibril formation, Beta-peptide, invitro, polymeric, nanoparticles, conformational-changes, molecular chaperone, adsorption, inhibition
National Category
Physical Chemistry
Identifiers
URN: urn:nbn:se:hkr:diva-21732DOI: 10.1021/la203078wISI: 000299366500024PubMedID: 22168533OAI: oai:DiVA.org:hkr-21732DiVA, id: diva2:1539752
Funder
Swedish Research CouncilThe Crafoord FoundationAvailable from: 2021-03-25 Created: 2021-03-25 Last updated: 2021-03-26Bibliographically approved

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CiteExportLink to record
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