Investigation on bindings of a binaphthoquinone derivative with serum albumin proteins by fluorescence spectroscopy

Jali, Bigyan Ranjan


Binding of a binaphthoquinone derivative namely, 5a,5b-dimethyldibenzo[b,h]biphenylene-5,6,11,12(5aH,5bH,11aH,11bH)-tetraone (L, C22H16O4)  with bovine serum albumin (BSA) and human serum albumin (HSA) have been examined by using fluorescence spectroscopy. The fluorescence emission of the L is quenched upon addition of L to a solution of  BSA or that of HSA, but the BSA has shown a higher affinity towards L over  the HSA protein. A molecular docking study is also performed to suggest the sites of BSA  for weak interactions to bind the L. The docking analysis,  has revealed the N-H···O  hydrogen bonds of L with different  amino acid residues. The L is located at about 7.7Å  away from the Trp-213 which is the fluorescent unit of the BSA suggesting the role of environment of the tryptophan residue to be an important to have changed the emission intensities.


Quinone, BSA, HSA, fluorescence, docking

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