The Effect of Nanoparticles on Amyloid Aggregation Depends on the Protein Stability and Intrinsic Aggregation Rate
(2012) In Langmuir 28(3). p.1852-1857- 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 2010 7 (2), 521-532]. The aggregation process was... (More)
- 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 2010 7 (2), 521-532]. The aggregation process was monitored by thioflavin T fluorescence in the absence and presence of copolyrneric 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 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/2348953
- author
- Cabaleiro-Lago, Celia LU ; Szczepankiewicz, Olga LU and Linse, Sara LU
- organization
- publishing date
- 2012
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Langmuir
- volume
- 28
- issue
- 3
- pages
- 1852 - 1857
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000299366500024
- scopus:84856191510
- pmid:22168533
- ISSN
- 0743-7463
- DOI
- 10.1021/la203078w
- language
- English
- LU publication?
- yes
- id
- 570c621c-f6e8-4b30-b1ed-695e18f8a785 (old id 2348953)
- date added to LUP
- 2016-04-01 10:48:34
- date last changed
- 2023-11-10 05:47:01
@article{570c621c-f6e8-4b30-b1ed-695e18f8a785,
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 2010 7 (2), 521-532]. The aggregation process was monitored by thioflavin T fluorescence in the absence and presence of copolyrneric 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 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.}},
author = {{Cabaleiro-Lago, Celia and Szczepankiewicz, Olga and Linse, Sara}},
issn = {{0743-7463}},
language = {{eng}},
number = {{3}},
pages = {{1852--1857}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Langmuir}},
title = {{The Effect of Nanoparticles on Amyloid Aggregation Depends on the Protein Stability and Intrinsic Aggregation Rate}},
url = {{http://dx.doi.org/10.1021/la203078w}},
doi = {{10.1021/la203078w}},
volume = {{28}},
year = {{2012}},
}