Structural bioinformatics and molecular dynamics simulations studies of cathepsins as a potential target for drug discovery

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University of the Thai Chamber of Commerce. Research Support Office
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University of the Thai Chamber of Commerce
Date Issued
2012
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Text::Conference output::Conference proceedings::Conference paper
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English
Abstract
Prediction of threedimensional structure of cathepsins, and molecular dynamics simulations of cathepsin S were studied by interaction with the drug molecule with virtual screening 681,158 compounds from ZINC database. The result of study showed top 1 ranked was obtained with drug molecule ZINC 23215439 reaction with cathepsin S. This demonstrates that the active site of cathepsin S Cys25, His164 and binding site Gln19 and Gly 20 are essential for interactions of cathepsin SZINC 23215439inhibitor complex. CoulombSR and LennardJonesSRinteractions energy of amino acids and drug molecule ZINC code 23215439 which consisted in active site of cathepsin S have been evaluated.
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(2012) Procedia Computer Science
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University of the Thai Chamber of Commerce
Bibliographic Citation
Surapong Pinitglang, Ratchanee Saiprajong, T. Dussadee, Khanok Ratanakhanokchai (2012) Structural bioinformatics and molecular dynamics simulations studies of cathepsins as a potential target for drug discovery., 63-74.
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