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A Kinetic Study of Amyloid Formation: Fibril Growth and Length Distributions
Journal article   Open access

A Kinetic Study of Amyloid Formation: Fibril Growth and Length Distributions

John S. Schreck and Jian-Min Yuan
The journal of physical chemistry. B, v 117(21), pp 6574-6583
30 May 2013
DOI: https://doi.org/10.1021/jp401586p
PMID: 23638987
Featured in Collection :   UN Sustainable Development Goals @ Drexel
url
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8094221View
Accepted (AM)Open Access (License Unspecified),  Open

Abstract

Chemistry Chemistry, Physical Physical Sciences Science & Technology
We propose a kinetic model for the self-aggregation by amyloid proteins. By extending several well-known models for protein aggregation, the time evolution of aggregate concentrations containing r proteins, denoted c(r)(t), can be written in terms of generalized Smoluchowski kinetics. With this approach, we take into account all possible aggregation and fragmentation reactions involving clusters of any size. Correspondingly, an aggregate of size x + y could be formed by or break up into two smaller constituent aggregates of sizes x and y. The rates of each aggregation or fragmentation reaction, called kernels, are specified in terms of the aggregate size, and we solve c(r)(t) for large cluster sizes using numerical techniques. We show that by using Smoluchowski kinetics many pathways to fibrillation are possible and quantities, such as the aggregate length distribution at an arbitrary time, can be calculated. We show that the predicted results of the model are in agreement with the experimental observations.

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54 citations in Web of Science
57 citations in Scopus

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Web of Science research areas
Chemistry, Physical
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