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Quesada-Soriano, I., Parker, L.J., Primavera, A., Casas- Solvas, J.M., Vargas-Berenguel, A., Barón, C., Morton, C.J., Mazzetti, A.P., Lo Bello, M., Parker, M.W. and García-Fuentes, L. (2009) Influence of the H-site residue 108 on human glutathione transferase P1-1 ligand binding: Structure-thermodynamic relationships and thermal stability. Protein Science, 18, 2454-2470. doi:10.1002/pro.253

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• TITLE: Glutathione transferase-P1-1 binding with naturally occurring ligands: assessment by docking simulations

  AUTHORS: Anupam J. Das, Sreeda Chalil, Poonam Nigam, Pamela Magee, Omar Janneh, Richard Owusu-Apenten

  KEYWORDS: Glutathione Transferase; Docking; Vitamins; Phytochemicals

  JOURNAL NAME: Journal of Biophysical Chemistry, Vol.2 No.4, November 9, 2011

  ABSTRACT: 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.