Research Article | Volume: 6, Issue: 1, January, 2016

Determination of ligand position in aspartic proteases by correlating tanimoto coefficient and binding affinity with root mean square deviation

Sandra Megantara Maria Immaculata Iwo Jutti Levita Slamet Ibrahim   

Open Access   

Published:  Jan 26, 2016

DOI: 10.7324/JAPS.2016.600120
Abstract

The objective of this study was to develop and validate of Structure-Based Virtual Screening (SBVS) protocol which was used to select the best pose of inhibitor-aspartic protease complex interaction in the active sites of HIV-1 protease, plasmepsin I, II, and IV. Retrospective validation was performed on enhanced dataset of ligands and decoys (DUD-E) for HIV-1 protease. The crystal structures 1XL2, 3QS1, 1SME, and 1LS5 were obtained from Protein Data Bank. The protocol was then challenged to re-dock the ligands to its origin places in the active sites by correlating Tanimoto coefficient (Tc) and binding affinity (Ei) with Root Mean Square Deviation (RMSD). Enrichment factor at 1% false positives (EF1%) values for Tc and Ei were 18.26 and 9.03, respectively, while the Area Under Curve (AUC) values for Tc and Ei were 76.84 and 60.95. The SBVS protocol was valid and showed better virtual screening qualities in ligand identification for HIV-1 protease compared to the original protocol accompanying the release of DUD-E and showed its ability to reproduce the co-crystal pose in the HIV-1 protease, plasmepsin I, II, and IV to its origin places in the active sites.


Keyword:     HIV-1 protease inhibitor-aspartic protease plasmepsins structure-based virtual screening.


Citation:

Megantara S, Iwo MI, Levita J, Ibrahim S. Determination of ligand position in aspartic proteases by correlating tanimoto coefficient and binding affinity with root mean square deviation. J App Pharm Sci, 2016; 6 (01): 125-129.

Copyright:The Author(s). This is an open access article distributed under the Creative Commons Attribution Non-Commercial License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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