2014
DOI: 10.1016/j.jlumin.2014.02.009
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A combined spectroscopic and molecular docking study on site selective binding interaction of Toluidine blue O with Human and Bovine serum albumins

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Cited by 75 publications
(23 citation statements)
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“…Moreover, the collisional quenching affects the excitation state of the fluorophore upon contact with quencher, resulting in an unchanged absorption spectrum of lysozyme. However, the ground‐state complex formation between ligand and protein resulted in the change in absorption spectrum of lysozyme . Consequently, the alteration in the absorption spectra of lysozyme in the presence of TBO again authenticated the existence of static quenching mechanism, and these results corroborate well with emission spectral studies .…”
Section: Resultssupporting
confidence: 72%
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“…Moreover, the collisional quenching affects the excitation state of the fluorophore upon contact with quencher, resulting in an unchanged absorption spectrum of lysozyme. However, the ground‐state complex formation between ligand and protein resulted in the change in absorption spectrum of lysozyme . Consequently, the alteration in the absorption spectra of lysozyme in the presence of TBO again authenticated the existence of static quenching mechanism, and these results corroborate well with emission spectral studies .…”
Section: Resultssupporting
confidence: 72%
“…that absorption intensity of lysozyme increased with a small red shift of around 2 nm, upon the successive addition of TBO. The observed red shift indicated that the interaction of TBO with lysozyme leads to increase in the hydrophobicity of the microenvironment around aromatic amino acid residues in lysozyme . Moreover, the collisional quenching affects the excitation state of the fluorophore upon contact with quencher, resulting in an unchanged absorption spectrum of lysozyme.…”
Section: Resultsmentioning
confidence: 99%
“…Since the emission spectrum of HSA/BSA depends on the degree of exposure of the Trp residues to the solvent polarity and upon its proximity to specic quenching groups, the observed decrease in emission intensity could be attributed to the binding of AZA with HSA/BSA. 26 The above interpretations showed that the binding site of AZA on HSA/BSA is most probably located near the Trp residues of HSA (Trp-214) and BSA (Trp-213). 27 It is well known that quenching of uorescent macromolecule can occur due to IFE (Inner Filter Effect), collisional quenching and binding-related quenching.…”
Section: Resultsmentioning
confidence: 91%
“…Such interactions have been previously reported in similar photosensitizer–HSA complexes, including TBO. 77,78…”
Section: Resultsmentioning
confidence: 99%