title: Structural protein-ligand interaction fingerprints (SPLIF) for structure-based virtual screening: method and benchmark study.
abstract: Accurate and affordable assessment of ligand-protein affinity for structure-based virtual screening (SB-VS) is a standing challenge. Hence, empirical postdocking filters making use of various types of structure-activity information may prove useful. Here, we introduce one such filter based upon three-dimensional structural protein-ligand interaction fingerprints (SPLIF). SPLIF permits quantitative assessment of whether a docking pose interacts with the protein target similarly to a known ligand and rescues active compounds penalized by poor initial docking scores. An extensive benchmark study on 10 diverse data sets selected from the DUD-E database has been performed in order to evaluate the absolute and relative efficiency of this method. SPLIF demonstrated an overall better performance than relevant standard methods.
authors.affiliation: Center for Integrative Chemical Biology and Drug Discovery, Eshelman School of Pharmacy, University of North Carolina at Chapel Hill , Campus Box 7363, Chapel Hill, North Carolina 27599-7363, United States.
authors.forename: C
authors.initials: C
authors.lastname: Da
authors.forename: D
authors.initials: D
authors.lastname: Kireev
mesh_terms: D008024:Ligands; D062105:Molecular Docking Simulation; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
chemical_list: D008024:Ligands; D011506:Proteins