Interaction Entropy for protein-ligand hot spot predicition
作者单位：State Key Laboratory for Precision SpectroscopySchool of Chemistry and Molecular EngineeringEast China Normal University Department of ChemistryNew York University
会议名称：《第十三届全国量子化学会议》
会议日期：2017年
学科分类：1007[医学-药学(可授医学、理学学位)] 10[医学]
关 键 词：interaction entropy hot spot protein-ligand
摘 要：The theoretical calculation of protein-ligand binding free energy is a grand challenge in computational *** prediction of critical residues along with their specific and quantitative contributions to protein-ligand binding free energy is extremely helpful to reveal binding mechanisms and identify drug-like molecules that alter protein-ligand *** this paper,we propose an interaction entropy approach combined with the MM/GBSA method for solvation to compute residue-specific protein-ligand binding free *** the current approach,the entropic loss in binding free energy of individual residues is explicitly computed from MD simulation by using the interaction entropy *** this approach the entropic contribution to binding free energy is determined from fluctuation of the interaction in MD *** for an extensive set of ALK protein-ligand interaction systems showed that by including the entropic contribution,we can clearly find the hot spot residues,it is helpful for new drug design.