Efficient evaluation of binding free energy using continuum electrostatics solvation
| Title | Efficient evaluation of binding free energy using continuum electrostatics solvation |
| Publication Type | Journal Article |
| Year of Publication | 2004 |
| Authors | Huang D., Caflisch A. |
| Journal | Journal of Medicinal Chemistry |
| Volume | 47 |
| Issue | 23 |
| Pagination | 5791-5797 |
| Date Published | 2004 Nov 4 |
| Type of Article | Research Article |
| Keywords | Amyloid Precursor Protein Secretases, Endopeptidases, HIV Protease, HIV Protease Inhibitors, Models, Molecular, Protease Inhibitors, Protein Binding, Static Electricity, Thermodynamics |
| Abstract | The linear interaction energy (LIE) method is combined with energy minimization and finite-difference Poisson calculation of electrostatic solvation for the estimation of the absolute free energy of binding. A predictive accuracy of about 1.0 kcal/mol is obtained for 13 and 29 inhibitors of β-secretase (BACE) and HIV-1 protease (HIV-1 PR), respectively. The multiplicative coefficients for the van der Waals and electrostatic terms are not transferable between BACE and HIV-1 PR although they are both aspartic proteases. The present approach is about 2 orders of magnitude faster than previous LIE methods and can be used for ranking large libraries of structurally diverse compounds docked by automatic computational tools. |
| DOI | 10.1021/jm049726m |
| pubindex | 0061 |
| Alternate Journal | J. Med. Chem. |
| PubMed ID | 15509178 |
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