2016
DOI: 10.1002/jmr.2532
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Biomolecular interaction study of hydralazine with bovine serum albumin and effect of β‐cyclodextrin on binding by fluorescence, 3D, synchronous, CD, and Raman spectroscopic methods

Abstract: Spectrofluoremetric technique was employed to study the binding behavior of hydralazine with bovine serum albumin (BSA) at different temperatures. Binding study of bovine serum albumin with hydralazine has been studied by ultraviolet-visible spectroscopy, fluorescence spectroscopy and confirmed by three-dimensional, synchronous, circular dichroism, and Raman spectroscopic methods. Effect of β-cyclodextrin on binding was studied. The experimental results showed a static quenching mechanism in the interaction of… Show more

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Cited by 10 publications
(7 citation statements)
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“…The fluorescence intensity of peak ‘a’ was found to increase with the addition of complexes owing to the interaction between BSA and complexes 1 – 3 . That means that the diameter of the macromolecule increased and resulted in the increase of the scattering effect . Peak ‘b’ mainly represents the spectral behaviour of the tryptophan and tyrosine residues, the maximum emission wavelength and fluorescence intensity of which are closely correlated with the polarity of their microenvironments.…”
Section: Resultsmentioning
confidence: 83%
“…The fluorescence intensity of peak ‘a’ was found to increase with the addition of complexes owing to the interaction between BSA and complexes 1 – 3 . That means that the diameter of the macromolecule increased and resulted in the increase of the scattering effect . Peak ‘b’ mainly represents the spectral behaviour of the tryptophan and tyrosine residues, the maximum emission wavelength and fluorescence intensity of which are closely correlated with the polarity of their microenvironments.…”
Section: Resultsmentioning
confidence: 83%
“…The fluorescence intensity of peak “a” was found to be increased with the addition of the complex. That is to say, the diameter of the macromolecule increased and concluded the increment of scattering effect . Peak “b” displays the spectral behavior of the tryptophan and tyrosine residues, the maximum emission wavelength and the fluorescence intensity of which are closely correlated with the polarity of their microenvironments.…”
Section: Resultsmentioning
confidence: 99%
“…Three‐dimensional fluorescence spectra and synchronous fluorescence spectra can provide information about the conformational changes of pepsin and trypsin with TF addition . For pepsin (Figure S1), as TF addition, the maximum peak (λ ex /λ em = 280/340 nm) was quenched by a ratio of 0.915 with a slightly red shift (Table ).…”
Section: Resultsmentioning
confidence: 99%