Study the interaction between CdTe@glutathione and human serum albumin

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...

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Bibliographic Details
Published inJournal of luminescence Vol. 135; pp. 335 - 338
Main Authors Yang, Qing, Zhou, Xi-min, Zhu, Yi-shuo, Chen, Xing-guo
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier B.V 01.03.2013
Elsevier
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Summary: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. ► In this paper, the binding of the CdTe@GSH QDs to human serum albumin (HSA) was studied using a fluorescence spectroscopy. ► The quenching mechanism was investigated in terms of the association constants and basic thermodynamic parameters. ► Furthermore, alteration of the secondary protein structure in the presence of the QDs was confirmed by synchronous fluorescence spectra. ► The research can help us assess biological toxicity of QDs and further expand the application scope of QDs.
ISSN:0022-2313
1872-7883
DOI:10.1016/j.jlumin.2012.09.015