Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/57669
Full metadata record
DC FieldValueLanguage
dc.contributor.authorBaruah, Jubaraj B-
dc.contributor.authorJali, Bigyan R-
dc.date.accessioned2021-07-07T11:02:16Z-
dc.date.available2021-07-07T11:02:16Z-
dc.date.issued2021-06-
dc.identifier.issn0975-0975(Online); 0376-4710(Print)-
dc.identifier.urihttp://nopr.niscair.res.in/handle/123456789/57669-
dc.description824-829en_US
dc.description.abstractBinding 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.en_US
dc.language.isoenen_US
dc.publisherCSIR-NIScPR, Indiaen_US
dc.sourceIJC-A Vol.60A(06) [June 2021]en_US
dc.subjectNaphthoquinoneen_US
dc.subjectFluorescenceen_US
dc.subjectBSAen_US
dc.subjectHSAen_US
dc.subjectMolecular dockingen_US
dc.titleInvestigation on bindings of a binaphthoquinone derivative with serum albumin proteins by fluorescence spectroscopyen_US
dc.typeArticleen_US
dcterms.publisherCSIR-NIScPR, Indiaen_US
dcterms.sourceIJC-A Vol.60A(06) [June 2021]
Appears in Collections:IJC-A Vol.60A(06) [June 2021]

Files in This Item:
File Description SizeFormat 
IJCA-60A(6) 824-829.pdfMain article1.21 MBAdobe PDFView/Open
IJCA-(824-829)_SI.pdfSupplementary Data387.76 kBAdobe PDFView/Open


Items in NOPR are protected by copyright, with all rights reserved, unless otherwise indicated.