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Evidence-Based Complementary and Alternative Medicine
Volume 2014 (2014), Article ID 450592, 20 pages
http://dx.doi.org/10.1155/2014/450592
Research Article

In Silico Insight into Potent of Anthocyanin Regulation of FKBP52 to Prevent Alzheimer’s Disease

1Department of Biomedical Informatics, Asia University, Taichung 41354, Taiwan
2School of Chinese Medicine, College of Chinese Medicine, China Medical University, Taichung 40402, Taiwan
3Department of Biotechnology, Asia University, Taichung 41354, Taiwan
4Department of Biological Science and Technology, China Medical University, Taichung 40402, Taiwan
5School of Medicine, College of Medicine, China Medical University, Taichung 40402, Taiwan

Received 21 October 2013; Revised 3 January 2014; Accepted 3 January 2014; Published 12 May 2014

Academic Editor: Fuu-Jen Tsai

Copyright © 2014 Tzu-Chieh Hung et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Alzheimer’s disease (AD) is caused by the hyperphosphorylation of Tau protein aggregation. FKBP52 (FK506 binding protein 52) has been found to inhibit Tau protein aggregation. This study found six different kinds of anthocyanins that have high binding potential. After analyzing the docking positions, hydrophobic interactions, and hydrogen bond interactions, several amino acids were identified that play important roles in protein and ligand interaction. The proteins’ variation is described using eigenvectors and the distance between the amino acids during a molecular dynamics simulation (MD). This study investigates the three loops based around Glu85, Tyr113, and Lys121—all of which are important in inducing FKBP52 activation. By performing a molecular dynamic simulation process between unbound proteins and the protein complex with FK506, it was found that ligand targets that docked onto the FK1 domain will decrease the distance between Glu85/Tyr113 and Glu85/Lys121. The FKBP52 structure variation may induce FKBP52 activation and inhibit Tau protein aggregation. The results indicate that anthocyanins might change the conformation of FKBP52 during binding. In addition, the purple anthocyanins, such as cyanidin-3-glucoside and malvidin-3-glucoside, might be better than FK506 in regulating FKBP52 and treating Alzheimer’s disease.