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

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Title Investigation on bindings of a binaphthoquinone derivative with serum albumin proteins by fluorescence spectroscopy
 
Creator Baruah, Jubaraj B
Jali, Bigyan R
 
Subject Naphthoquinone
BSA
Fluorescence
Molecular docking
HSA
 
Description 824-829
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.
 
Date 2021-07-05T11:46:59Z
2021-07-05T11:46:59Z
2021-06
 
Type Article
 
Identifier 0975-0975(Online); 0376-4710(Print)
http://nopr.niscair.res.in/handle/123456789/57622
 
Language en
 
Publisher CSIR-NIScPR, India
 
Source JC-A Vol.60A(06) [June 2021]