MODULATORY ROLE OF CITRAL ON HEAT SHOCK PROTEINS WITH SPECIAL REFERENCE TO HSP90 FROM YEAST

VINJAMURI S.¹, GAONKAR R.^2
1Department of Biotechnology, BMS College of Engineering, Basavanagudi, Bangalore- 560 019, Karnataka, India.
²Department of Biotechnology, BMS College of Engineering, Basavanagudi, Bangalore- 560 019, Karnataka, India.

Received : 07-07-2014     Accepted : 24-07-2014     Published : 05-08-2014
Volume : 3     Issue : 1       Pages : 66 - 70
World Res J Biochem 3.1 (2014):66-70

Heat shock proteins (HSPs), which act as molecular chaperones assist a nascent polypeptide chain to attain a functional conformation and then bring the protein to the cellular site where it carries out its functions. The molecular chaperone HSP90 is reported to assist in proper folding of various client proteins which are involved in oncogenesis. This occurs by ATPase activity of the N-terminal domain of HSP90.So the inhibitors of ATPase activity of HSP90 are sought by the scientific community for the treatment of various cancers. Citral which is the major component of lemon grass oil is reported to induce apoptosis of cancer cells. Here we have reported the binding studies of citral with HSP90 ATP/ADP binding site of yeast. The docking studies were carried out using Arguslab 4.0. The findings of the docking studies show that binding energy of citral with yeast HSP90 was -9.41 kcal/mol which was comparable with its binding energy with human HSP90(-8.65 kcal/mol) and HSP90 of Plasmodium falciparum (-9.11kcal/mol).