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Bioinorganic Chemistry and Applications
Volume 2008, Article ID 469062, 6 pages
http://dx.doi.org/10.1155/2008/469062
Research Article

The Crystal Water Affect in the Interaction between the Tenebrio Molitor Alpha-Amylase and Its Inhibitor

1School of Chemical and Material Engineering, Jiangnan University, Wuxi, Jiangsu 214122, China
2Institute of Microbiology, Chinese Academy of Sciences, Beijing 100080, China

Received 5 November 2007; Revised 22 January 2008; Accepted 4 March 2008

Academic Editor: Konstantinos Tsipis

Copyright © 2008 Zhu Zhi-Fei 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

Molecular dynamics simulation of the interaction between the Tenebrio molitor alpha-amylase and its inhibitor at different proportion of crystal water was carried out with OPLS force field by hyperchem 7.5 software. In the correlative study, the optimal temperature of wheat monomeric and dimeric protein inhibitors was from 273 K to 318 K. The the average temperature of experimentation is 289 K. (1) The optimal temperature of interaction between alpha-amylase and its inhibitors was 280 K without crystal water that was close to the results of experimentation. The forming of enzyme-water and inhibitor-water was easy, but incorporating third monomer was impossible. (2) Having analyzed the potential energy data, the optimal temperature of interaction energy between alpha-amylase and its inhibitors covering 9 : 1, 5 : 5, 4 : 6, and 1 : 9 proportion crystal water was 290 K. (3) We compared the correlative QSAR properties. The proportion of crystal water was close to the data of polarizability (12.4%) in the QSAR properties. The optimal temperature was 280 K. This result was close to 289 K. These findings have theoretical and practical implications.