Uttam Pal - Nickel(II)-Schiff base complex recognizing domain II of bovine and human serum albumin: spectroscopic and docking studies

Document created by Uttam Pal on Dec 25, 2015
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  Publication Details (including relevant citation   information):

  Ray, Aurkie, Seth, Banabithi Koley, Pal, Uttam, Basu, Samita   92 164-174

  Abstract: It has been spectroscopically   monitored that a mononuclear nickel(II)-Schiff base complex   {[NiL]·CH(3)OH=NSC} exhibits greater binding affinity for bovine   serum albumin (BSA) than that of its human counterpart (HSA).   Moreover the modes of binding of NSC with the two serum albumins   also differ significantly. Docking studies predict a relatively   rare type of 'superficial binding' of NSC at domain IIB of HSA   with certain mobility whereas for BSA such phenomena has not been   detected. The mobile nature of NSC at domain IIB of HSA has been   well correlated with the spectroscopic results. It is to be noted   that thermodynamic parameters for the NSC interaction also differ   for the two serum albumins. Occurrence of energy transfer between   the donor (Trp of BSA and HSA) and acceptor (NSC) has been   obtained by means of Förster resonance energy transfer (FRET).   The protein stability on NSC binding has also been experimented   by the GuHCl-induced protein unfolding studies. Interestingly it   has been found that NSC-HSA interaction enhances the protein   stability whereas NSC-BSA binding has no such impact. Such   observations are indicative of the fact that the conformation of   NSC is responsible in recognizing the two serum albumins and   selectively enhancing protein stability.

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