The Crystal Water affect in the Interaction between the Tenebrio Mollitor Alpha-amylase and Its Inhibitor

摘要

In this paper, molecular dynamics simulation of the interaction between the tenebrio mollitor 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 273K to 318K.The the average temperature of experimentation is 289K. (1) The optimal temperature of interaction between alpha-amylase and its inhibitors was 280K without crystal water that was close to the results of experimentation .The forming of enzyme -water and inhibitor- water was easy, but the incorporating third monomer was impossible. (2) 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 290K. (3) 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 280K. This result was close to 289K. These findings have theoretical and practical implications.