Rapid and accurate estimation of protein-ligand relative binding affinities using site-identification by ligand competitive saturation.

ABSTRACT: Predicting relative protein-ligand binding affinities is a central pillar of lead optimization efforts in structure-based drug design. The site identification by ligand competitive saturation (SILCS) methodology is based on functional group affinity patterns in the form of free energy maps that may be used to compute protein-ligand binding poses and affinities. Presented are results obtained from the SILCS methodology for a set of eight target proteins as reported originally in Wang et al. (J. Am. Chem. Soc., 2015, 137, 2695-2703) using free energy perturbation (FEP) methods in conjunction with enhanced sampling and cycle closure corrections. These eight targets have been subsequently studied by many other authors to compare the efficacy of their method while comparing

SUBMITTER: Goel H 

PROVIDER: S-EPMC8246086 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature