Abstract
In this paper, glutathione (GSH) modified CdTe quantum dots (CdTe@GSH QDs) were synthesized in an aqueous solution. Then, the binding of the CdTe@GSH QDs to human serum albumin (HSA) was studied using the fluorescence spectroscopy. The quenching mechanism was investigated in terms of the association constants and basic thermodynamic parameters. The fluorescence data revealed that CdTe@GSH QDs could quench the intrinsic fluorescence of human serum albumin by a static quenching mechanism. Furthermore, alteration of the secondary protein structure in the presence of the QDs was confirmed by synchronous fluorescence spectra.
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