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  • Title: Spectroscopic investigation of water-soluble alloyed QDs with bovine serum albumin.
    Author: Adarsh KS, Singh MK, Kotresh MG, Inamdar LS, Shivkumar MA, Jagatap BN, Mulimani BG, Inamdar SR.
    Journal: Luminescence; 2017 Feb; 32(1):35-42. PubMed ID: 27118686.
    Abstract:
    We present here a systematic investigation on the interaction between a water-soluble alloyed semiconductor quantum dot and bovine serum albumin using various spectroscopic techniques i.e. fluorescence quenching, resonance light scattering and synchronous fluorescence spectroscopy. The analysis of fluorescence spectrum and fluorescence intensity indicates that the intrinsic fluorescence of bovine serum albumin (BSA) gets quenched by both static and dynamic quenching mechanism. The Stern-Volmer quenching constants, energy transfer efficiency parameters, binding parameters and corresponding thermodynamic parameters (ΔH0 , ΔS0 and ΔG0 ) have been evaluated by using van 't Hoff equation at different temperatures. A positive entropy change with a positive enthalpy change was observed suggesting that the binding process was an entropy-driven, endothermic process associated with the hydrophobic effect. The intermolecular distance (r) between donor (BSA) and acceptor (CdSeS/ZnS quantum dots) was estimated according to Förster's theory of non-radiative energy transfer. The synchronous fluorescence spectra revealed a blue shift in the emission maxima of tryptophan which is indicative of increasing hydrophobicity. Negative ΔG0 values implied that the binding process was spontaneous. It was found that hydrophobic forces played a role in the quenching process. Copyright © 2016 John Wiley & Sons, Ltd.
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