Analysis of electrostatic and hydrophobic complementarities between trypsin and Cucurbita maxima trypsin inhibitor I using molecular electrostatic potential

Abstract

The molecular electrostatic potential (MEP) and MEP correlation were calculated for the trypsin and Cucurbita maxima trypsin inhibitor I system using the method of rapid evaluation of MEP for large biological molecules, and the enzyme-inhibitor interaction was analyzed on the basis of electrostatic and hydrophobic complementarities. The calculated electrostatic complementarity is conspicuously large in the p 1 region of the inhibitor and the hydrophobic complementarity is large at the P 1′ position, and these large complementarities promote the binding process of the inhibitor. It was demonstrated that the MEP and MEP correlation were used effectively for quantitative analysis of enzyme-substrate interactions.