Spectroscopic investigation of water-soluble alloyed QDs with bovine serum albumin

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• 作者：K. S. Adarsh ; M. K. Singh ; M. G. Kotresh ; Laxmi S. Inamdar ; M. A. Shivkumar ; B. N. Jagatap ; B. G. Mulimani and S. R. Inamdar
• 刊名：Luminescence
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：32
• 期：1
• 页码：35-42
• 全文大小：790K
• ISSN：1522-7243

文摘

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