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Article citations


Hashimoto, M., Shahdat, H.M., Yamashita, S., Katakura, M., Tanabe, Y., Fujiwara ,H., Gamoh, S., Miyazawa, T., Arai H., Shimada, T. and Shido, O. (2008) Docosahexaenoic Acid Disrupts in Vitro Amyloid Beta(1-40)Fibrillation and Concomitantly Inhibits Amyloid Levels in Cerebral Cortex of Alzheimer’s Disease Modelrats. Journal of Neurochemistry, 107, 1634-1646.

has been cited by the following article:

  • TITLE: Computational Analyses of Docosahexaenoic Acid (DHA, C22:6, n-3) with Alzheimer’s Disease-Causing Amyloid Peptide Aβ1-42 Reassures Its Therapeutic Utility

    AUTHORS: Michio Hashimoto, Shahdat Hossain, Kentaro Matsuzaki, Abdullah Al Mamun, Hiroyuki Arai, Osamu Shido

    KEYWORDS: Docosahexaenoic Acid, Alzheimer’s Disease, Amyloid Beta Peptide, Molecular Docking, In Silico, Drug Design, Protein Data Bank

    JOURNAL NAME: Advances in Alzheimer's Disease, Vol.5 No.2, June 29, 2016

    ABSTRACT: The accumulation of amyloid β peptide1-42 (Aβ1-42) masses in the brains of Alzheimer’s Disease (AD) patients is associated with neuronal loss and memory deficits. We have previously reported that oral administration of docosahexaenoic acid (DHA, C22:6, n-3) significantly decreases Aβ burden in the brains of AD model rats and that direct in vitro incubation of DHA with Aβ1-42 curbs the progression of amyloid fibrillation. In the present in silico study, we investigated whether DHA computationally binds with amyloid peptides. The NMR solution structures of Aβ1-42 were downloaded from the Protein Data Bank (PDB IDs: 1Z0Q and 2BEG). The binding of DHA to Aβ peptides was assessed by molecular docking using both a flexible and rigid docking system. Thioflavin T (ThT) was used as positive control. The chemical structures of ThT and DHA were modeled and converted to the PDB format using PRODRUG. Drug-like properties of DHA were evaluated by ADME (Absorption, Distribution, Metabolism, and Excretion). DHA was found to successfully dock with Aβ1-42. Computational analyses of the binding of DHA to Aβ1-42, as evaluated by docking studies, further corroborated the inhibitory effect of DHA on in vitro Aβ1-42 fibrillogenesis and might explain the in vivo reduction of amyloid burden observed in the brains of DHA-administered AD model rats demonstrated in our previous study. These computational data suggest the potential utility of DHA as a preventive medication in Aβ-induced neurodegenerative diseases, including AD.