Das, Anupam J., Chalil, Sreeda, Nigam, P, Magee, Pamela, Janneh, Omar and Owusu-Apenten, Richard (2011) Glutathione transferase-P1-1 binding with naturally occurring ligands: assessment by docking simulations. Journal of Biophysical Chemistry, 02 (04). pp. 401-407. [Journal article]
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Glutathione transferase-P1-1 (hGSTP1-1), which is associated with acquired drug resistance in some tumour cells, requires two identical subunits for full activity. Naturally occurring inhibitors for GSTP1-1 quaternary structure could be interesting therapeutic agents. The aim of this study was to investigate potential binding sites for hGSTP1-1 interaction with ligands many of which occur naturally. Simulations were performed with commercial docking software and with GST monomer or dimer as template. Docking results using hGSTP1-1 dimer showed one binding site for most of the ligands tested. Lycopene, glutathione, ellagic acid, ethacrynic acid, quercetin, caffeic acid, ferulic acid, porphyrin, curcumin, cinnamic acid, and also α-tocopherol bound at the enzyme dimer subunit-subunit interface. In contrast, investigations using hGSTP1-1 monomer revealed three additional sites for ligand binding. In conclusion, the docking simulations suggest that the enzyme subunit interface may be important for hGSTP1-1 interactions with ligands. These findings may provide valuable insights for further research to identify naturally occurring therapeutic agents.
|Item Type:||Journal article|
|Faculties and Schools:||Faculty of Life and Health Sciences|
Faculty of Life and Health Sciences > School of Biomedical Sciences
|Research Institutes and Groups:||Biomedical Sciences Research Institute|
Biomedical Sciences Research Institute > Infection and Immunity/Microbiology
Biomedical Sciences Research Institute > Northern Ireland Centre for Food and Health (NICHE)
|Deposited By:||Dr Richard Owusu-Apenten|
|Deposited On:||09 May 2012 11:51|
|Last Modified:||18 Dec 2012 17:01|
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