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Stochastic kinetic study of protein aggregation and molecular crowding effects of Aβ40 and Aβ42
Journal article   Peer reviewed

Stochastic kinetic study of protein aggregation and molecular crowding effects of Aβ40 and Aβ42

JOURNAL OF THE CHINESE CHEMICAL SOCIETY, v 70(3), p579
Mar 2023
DOI: https://doi.org/10.1002/jccs.202200365
Featured in Collection :   UN Sustainable Development Goals @ Drexel

Abstract

Two isoforms of beta-amyloid peptides, A beta 40 and A beta 42, differ from each other only in the last two amino acids, IA, at the end of A beta 42. They, however, differ significantly in their ability in inducing Alzheimer's disease (AD). The rate curves of fibril growth of A beta 40 and A beta 42 and the effects of molecular crowding have been measured in in vitro experiments. These experimental curves, on the other hand, have been fitted in terms of rate constants for elementary reaction steps using rate equation approaches. Several sets of such rate parameters have been reported in the literature. Employing a recently developed stochastic kinetic method, implemented in a browser-based simulator, popsim, we study to reveal the differences in the kinetic behaviors implied by these sets of rate parameters. In particular, the stochastic method is used to distinguish the kinetic behaviors between A beta 40 and A beta 42 isoforms. As a result, we make general comments on the usefulness of these sets of rate parameters.

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UN Sustainable Development Goals (SDGs)

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#3 Good Health and Well-Being

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Collaboration types
Domestic collaboration
Web of Science research areas
Chemistry, Multidisciplinary
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