The Molecular Dynamics Simulation Of The Interaction Between The Tenebrio Mollitor Alpha-amylase And Its Inhibitor Or Amylose 20

In this paper, molecular dynamics simulation of the interaction between the Tenebrio mollitor alpha-amylase and amylase 20 or its inhibitor at different proportion of crystal water was carried out with OPLS force field by hyperchem 7.5 software. Compared the correlative QSAR properties, the optimal temperature of interaction between alpha-amylase and amylase 20 or its inhibitors were obtained.As the interaction between the Tenebrio mollitor alpha-amylase and amylase 20, (1) The optimal temperature of interaction between alpha-amylase and amylase 20 was 330K without crystal water that was close to the results of experimentation. As temperature increase, the interaction energy between alpha-amylase and amylase 20 tends to get smaller. The forming amylase 20 - water was hard, but the incorporating enzyme was easy. The forming of enzyme–water was easy, but the incorporating amylase 20 was impossible. (2)Analyzed the potential energy data, the interaction energy between alpha-amylase and amylose 20 was on the nadir at 320K, 340K when the proportion of crystal water was 5:5 and 4:6 respectively. (3)Compared the correlative QSAR properties, this proportion of crystal water was close to the data of Refractivity (9.7%) and Polarizability (9.5%) in the QSAR properties. The optimal temperature was 340K.People is very interested in which mechanism and optimal condition of inhibitor exerted on alpha-amylases. The result of simulation of the interaction between the Tenebrio mollitor alpha-amylase and its inhibitor as follows: (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. In the correlative study, the optimal temperature of Wheat Monomeric and Dimeric Protein Inhibitors was from 273K to 318K. These findings have theoretical and practical implications.