2015
DOI: 10.1016/j.colsurfb.2015.06.010
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Fluorescence behavior of globular proteins from their bulk and thin film conformations in presence of mono-, di- and tri-valent ions

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Cited by 12 publications
(5 citation statements)
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“…As expected, the fluorescence intensity of VEGF-N,S-CDs increased at a higher VEGF concentration used for its conjugation to the N,S-CDs. 56,57 The enhancement in the fluorescence intensity of VEGF-N,S-CDs at a higher VEGF conjugation density occurred due to the stronger surface passivation of CDs and higher surface hydrophobicity 58 as a result of elimination of some nonradiative transitions 45,59,60 or suppressed quenching resulting from interactions with solvent or ions. A similar effect was observed for semiconductor and carbon quantum dots conjugated to proteins.…”
Section: ■ Results and Discussionmentioning
confidence: 99%
“…As expected, the fluorescence intensity of VEGF-N,S-CDs increased at a higher VEGF concentration used for its conjugation to the N,S-CDs. 56,57 The enhancement in the fluorescence intensity of VEGF-N,S-CDs at a higher VEGF conjugation density occurred due to the stronger surface passivation of CDs and higher surface hydrophobicity 58 as a result of elimination of some nonradiative transitions 45,59,60 or suppressed quenching resulting from interactions with solvent or ions. A similar effect was observed for semiconductor and carbon quantum dots conjugated to proteins.…”
Section: ■ Results and Discussionmentioning
confidence: 99%
“…To understand the possible nature of interactions via fluorescence quenching, S-V curves are plotted and the data are analyzed using the S-V equation [43,44] where, F 0 is the fluorescence intensity of the fluorophore in the absence of a quenching material, i.e. ions in our study, F is fluorescence intensity of the fluorophore in the presence of ions, M is the concentration of ions, k q is the quenching rate constant, τ 0 is the lifetime of fluorophore in the absence of a quencher and K sv is the S-V quenching constant.…”
Section: Fluorescence Quenching Studymentioning
confidence: 99%
“…Globular protein exhibits uorescence property due to the presence of tryptophan and tyrosine amino acid residues. Protein-protein interaction can also be explained by studying the uorescence properties of the proteins [40,41]. In our previous work, we observed the enhancement of uorescence emission in the re-entrant region, and it was correlated with the hydrodynamic size as well as mobility of the protein [42].…”
Section: Introductionmentioning
confidence: 97%