Spectroscopy of nanomaterials

What is it about?

We present here a systematic investigation on the interaction between a water-soluble alloyed semiconductor nanoparticles and a protein - bovine serum albumin using spectroscopic techniques i.e., absorption, 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. Thermodynamic study yielded positive entropy change with a positive enthalpy change suggesting that the binding process was an entropy-driven, endothermic process associated with the hydrophobic effect. 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.

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