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Crowding effects on amyloid aggregation kinetics


Magno, A; Caflisch, A; Pellarin, R (2010). Crowding effects on amyloid aggregation kinetics. Journal of Physical Chemistry Letters, (1):3027-3032.

Abstract

Biological protein self-assembly occurs in the cellular milieu, densely occupied by other macromolecules which do not participate directly in the aggregation process. Excluded volume effects arising in such a crowded environment deeply affect the thermodynamics and kinetics of biological processes, like protein folding, ligand binding, and protein aggregation. Here, Langevin dynamics
simulations of a simplified model of an amphipathic polypeptide are used to investigate how macromolecular crowding influences the amyloid aggregation
kinetics. The simulations show that the net influence of macromolecular crowding on the self-assembly process is the result of two competing effects: oligomer stabilization and solution viscosity increase. Notably, the net effect crucially depends on the aggregation propensity and pathways. Therefore, comparative studies of concentration and crowding effects on the kinetics of amyloid aggregation
could shed light on the underlying self-assembly mechanism.

Abstract

Biological protein self-assembly occurs in the cellular milieu, densely occupied by other macromolecules which do not participate directly in the aggregation process. Excluded volume effects arising in such a crowded environment deeply affect the thermodynamics and kinetics of biological processes, like protein folding, ligand binding, and protein aggregation. Here, Langevin dynamics
simulations of a simplified model of an amphipathic polypeptide are used to investigate how macromolecular crowding influences the amyloid aggregation
kinetics. The simulations show that the net influence of macromolecular crowding on the self-assembly process is the result of two competing effects: oligomer stabilization and solution viscosity increase. Notably, the net effect crucially depends on the aggregation propensity and pathways. Therefore, comparative studies of concentration and crowding effects on the kinetics of amyloid aggregation
could shed light on the underlying self-assembly mechanism.

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27 citations in Web of Science®
24 citations in Scopus®
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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
Dewey Decimal Classification:570 Life sciences; biology
Date:2010
Deposited On:24 Mar 2011 16:31
Last Modified:05 Apr 2016 14:53
Publisher:American Chemical Society
ISSN:1948-7185
Publisher DOI:https://doi.org/10.1021/jz100967z

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