Effect of mutation on Aβ1-42-Heme complex in aggregation mechanism: Alzheimer's disease
S Boopathi, P Kolandaivel - Journal of Molecular Graphics and Modelling, 2017 - Elsevier
Amyloid β (Aβ) peptide aggregation is one of the root causes for Alzheimer's disease.
Recently, experimental studies show that three active binding sites (His6, His13 and His14)
of Aβ peptides were bound with heme to form Aβ-Heme complex, which leads to inhibit the
aggregation process. We apply molecular dynamic simulation to investigate the aggregation
pathways of Aβ-Heme peptides. The above three binding sites were mutated by Glycine
residue individually and generate three complex systems such as Aβ (His6Gly)-Heme, Aβ …
Recently, experimental studies show that three active binding sites (His6, His13 and His14)
of Aβ peptides were bound with heme to form Aβ-Heme complex, which leads to inhibit the
aggregation process. We apply molecular dynamic simulation to investigate the aggregation
pathways of Aβ-Heme peptides. The above three binding sites were mutated by Glycine
residue individually and generate three complex systems such as Aβ (His6Gly)-Heme, Aβ …
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