Evaluating the ability of end-point methods to predict the binding affinity tendency of protein kinase inhibitors.

ABSTRACT: Because of the high economic cost of exploring the experimental impact of mutations occurring in kinase proteins, computational approaches have been employed as alternative methods for evaluating the structural and energetic aspects of kinase mutations. Among the main computational methods used to explore the affinity linked to kinase mutations are docking procedures and molecular dynamics (MD) simulations combined with end-point methods or alchemical methods. Although it is known that end-point methods are not able to reproduce experimental binding free energy (ΔG) values, it is also true that they are able to discriminate between a better or a worse ligand through the estimation of ΔG. In this contribution, we selected ten wild-type and mutant cocrystallized EGFR-inhibitor

SUBMITTER: Bello M 

PROVIDER: S-EPMC10443623 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature