The initial stage of structural transformation of Aβ
Alzheimer’s diseases
Human and rat amyloid beta 42
Metal irons
Molecular dynamics simulation
Protein folding
Journal
Computational biology and chemistry
ISSN: 1476-928X
Titre abrégé: Comput Biol Chem
Pays: England
ID NLM: 101157394
Informations de publication
Date de publication:
Dec 2019
Dec 2019
Historique:
received:
15
04
2019
revised:
10
09
2019
accepted:
13
09
2019
pubmed:
5
10
2019
medline:
20
12
2019
entrez:
5
10
2019
Statut:
ppublish
Résumé
The early stage of secondary structural conversion of amyloid beta (Aβ) to misfolded aggregations is a key feature of Alzheimer's disease (AD). Under normal physiological conditions, Aβ peptides can protect neurons from the toxicity of highly concentrated metals. However, they become toxic under certain conditions. Under conditions of excess iron, amyloid precursor proteins (APP) become overexpressed. This subsequently increases Aβ production. Experimental studies suggest that Aβ fibrillation (main-pathway) and amorphous (off-pathway) aggregate formations are two competitive pathways driven by factors such as metal binding, pH and temperature. In this study, we performed molecular dynamic (MD) simulations to examine the initial stage of conformational transformations of human Aβ (hAβ) and rat Aβ (rAβ) peptides in the presence of Fe
Identifiants
pubmed: 31585353
pii: S1476-9271(19)30326-3
doi: 10.1016/j.compbiolchem.2019.107128
pii:
doi:
Substances chimiques
Amyloid beta-Peptides
0
Ferric Compounds
0
Ferrous Compounds
0
Protein Aggregates
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
107128Informations de copyright
Copyright © 2019 Elsevier Ltd. All rights reserved.