A Mathematical Model for Amyloid-ð· Aggregation in the Presence of Metal Ions: A Timescale Analysis for the Progress of Alzheimer Disease.
Bull Math Biol
; 81(6): 1943-1964, 2019 06.
Article
em En
| MEDLINE
| ID: mdl-30809773
ABSTRACT
The aggregation of amyloid-ð½ (Að½) proteins through their self-assembly into oligomers, fibrils, or senile plaques is advocated as a key process of Alzheimer's disease. Recent studies have revealed that metal ions play an essential role in modulating the aggregation rate of amyloid-ð½ (Að½) into senile plaques because of high binding affinity between Að½ proteins and metal ions. In this paper, we proposed a mathematical model as a set of coupled kinetic equations that models the self-assembly of amyloid-ð½ (Að½) proteins in the presence of metal ions. The numerical simulations capture four timescales in the Að½ dynamics associated with three important events which include the formation of the amyloid-metal complex, the homogeneous aggregation of the amyloid-metal complexes, and the non-homogeneous aggregation of the amyloid-metal complexes. The method of singular perturbation is used to identify these timescales in the framework of slow-fast systems.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos beta-Amiloides
/
Doença de Alzheimer
/
Agregação Patológica de Proteínas
/
Modelos Biológicos
Tipo de estudo:
Etiology_studies
Limite:
Humans
Idioma:
En
Revista:
Bull Math Biol
Ano de publicação:
2019
Tipo de documento:
Article
País de afiliação:
Estados Unidos