Assembly of ligands interaction models for glutathione-S-transferases from Plasmodium falciparum, human and mouse using enzyme kinetics and molecular docking
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- 作者：Mohammed Nooraldeen Al-Qattana ; mohammed_alqattan@yahoo.com" class="auth_mail" title="E-mail the corresponding author ; Mohd Nizam Mordib ; Sharif Mahsofi Mansorb
- 关键词：Enzyme kinetics ; Molecular docking ; PfGST ; hGSTP1 ; mGSTM1
- 刊名：Computational Biology and Chemistry
- 出版年：2016
- 出版时间：October 2016
- 年：2016
- 卷：64
- 期：Complete
- 页码：237-249
- 全文大小：3121 K
文摘
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Binding modes and affinities for GST ligands were determined .
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Enzyme kinetic and docking studies were used in determination.
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GST isoforms studied include pfGST, hGSTP1, mGSTM1.
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Ligand–ligand interactions at PfGST binding sites were studied kinetically.
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The eligibility for given ligands as leads for GST inhibitors were discussed.