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

Conference proceedings article

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Author list: Pinitglang S., Saiprajong R., Dussadee T., Ratanakhanokchai K.

Publisher: Elsevier

Publication year: 2012

Volume number: 11

Start page: 63

End page: 74

Number of pages: 12

ISSN: 1877-0509

URL: https://www.scopus.com/inward/record.uri?eid=2-s2.0-84897032142&doi=10.1016%2fj.procs.2012.09.008&partnerID=40&md5=71e8153becd9b7230463852d47445136

Languages: English-Great Britain (EN-GB)

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Abstract

Prediction of three-dimensional 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 23215439 inhibitor complex. Coulomb-SR and Lennard-Jones-SR interactions energy of amino acids and drug molecule ZINC code 23215439 which consisted in active site of cathepsin S have been evaluated. ฉ 2012 Published by Elsevier Ltd.

Keywords

Cathepsin, Cysteine proteinase, Homology modeling, Virtual screening