title: A simple and efficient dispersion correction to the Hartree-Fock theory (2): Incorporation of a geometrical correction for the basis set superposition error.
abstract: One of the most challenging problems in computer-aided drug discovery is the accurate prediction of the binding energy between a ligand and a protein. For accurate estimation of net binding energy ΔEbind in the framework of the Hartree-Fock (HF) theory, it is necessary to estimate two additional energy terms; the dispersion interaction energy (Edisp) and the basis set superposition error (BSSE). We previously reported a simple and efficient dispersion correction, Edisp, to the Hartree-Fock theory (HF-Dtq). In the present study, an approximation procedure for estimating BSSE proposed by Kruse and Grimme, a geometrical counterpoise correction (gCP), was incorporated into HF-Dtq (HF-Dtq-gCP). The relative weights of the Edisp (Dtq) and BSSE (gCP) terms were determined to reproduce ΔEbind calculated with CCSD(T)/CBS or /aug-cc-pVTZ (HF-Dtq-gCP (scaled)). The performance of HF-Dtq-gCP (scaled) was compared with that of B3LYP-D3(BJ)-bCP (dispersion corrected B3LYP with the Boys and Bernadi counterpoise correction (bCP)), by taking ΔEbind (CCSD(T)-bCP) of small non-covalent complexes as 'a golden standard'. As a critical test, HF-Dtq-gCP (scaled)/6-31G(d) and B3LYP-D3(BJ)-bCP/6-31G(d) were applied to the complex model for HIV-1 protease and its potent inhibitor, KNI-10033. The present results demonstrate that HF-Dtq-gCP (scaled) is a useful and powerful remedy for accurately and promptly predicting ΔEbind between a ligand and a protein, albeit it is a simple correction procedure.
authors: Institute of Biomedical Sciences, Tokushima University, Graduate School, 1-78 Shomachi, Tokushima 770-8505, Japan.
authors: Tatsusada
authors: T
authors: Yoshida
authors: Institute of Biomedical Sciences, Tokushima University, Graduate School, 1-78 Shomachi, Tokushima 770-8505, Japan.
authors: Takahisa
authors: T
authors: Hayashi
authors: Institute of Biomedical Sciences, Tokushima University, Graduate School, 1-78 Shomachi, Tokushima 770-8505, Japan.
authors: Akira
authors: A
authors: Mashima
authors: Institute of Biomedical Sciences, Tokushima University, Graduate School, 1-78 Shomachi, Tokushima 770-8505, Japan. Electronic address: hchuman@tokushima-u.ac.jp.
authors: Hiroshi
authors: H
authors: Chuman
mesh_terms: D004305:Dose-Response Relationship, Drug; D016333:HIV Protease / Q000737:chemistry* / Q000378:metabolism; D017320:HIV Protease Inhibitors / Q000737:chemistry* / Q000378:metabolism; D007546:Isoquinolines / Q000737:chemistry* / Q000378:metabolism; D015394:Molecular Structure; D011485:Protein Binding; D011789:Quantum Theory; D013329:Structure-Activity Relationship; D013844:Thiazoles / Q000737:chemistry* / Q000378:metabolism
chemical_list: D017320:HIV Protease Inhibitors; D007546:Isoquinolines; C522501:KNI 10033; D013844:Thiazoles; D016333:HIV Protease
keywords: Basis set superposition error (BSSE); Density functional theory; Dispersion energy correction; Geometrical correction for BSSE; HIV-1 protease; Hartree–Fock theory; Protein–ligand interaction energy