Journal of Computer Chemistry, Japan
Online ISSN : 1347-3824
Print ISSN : 1347-1767
General Paper
Classical Molecular Dynamics Simulation to Understand Role of a Zinc Ion for Aggregation of Amyloid-β Peptides
Hiroaki NISHIZAWAHisashi OKUMURA
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2018 Volume 17 Issue 1 Pages 76-79

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Abstract

Metal ions such as those of copper and zinc are considered to accelerate initial formation of amyloid fibril of amyloid-β (Aβ) peptides. In this study, the role of a zinc ion for Aβ peptide aggregation was investigated by the classical molecular dynamics (MD) simulations. The MD results indicated that the negatively-charged residues gained large stabilization in the existence of a zinc ion. On the other hand, histidine and tyrosine which were reported as making a bond with a metal ion were slightly stabled. Therefore, a zinc ion is thought of as combining with histidine or tyrosine after being attracted by negatively-charged residues, because these residues exist near negatively-charged residues. These results indicate that the metal-containing system needs to be treated by quantum-mechanical techniques.

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© 2018 Society of Computer Chemistry, Japan
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