Study the interaction between CdTelutathione and human serum albumin

In this paper, glutathione (GSH) modified CdTe quantum dots (CdTeSH QDs) were synthesized in an aqueous solution. Then, the binding of the CdTeSH QDs to human serum albumin (HSA) was studied using the fluorescence spectroscopy. The quenching mechanism was investigated in terms of the association con...

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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 01.03.2013
Subjects
Cadmium tellurides
Constants
Fluorescence
Human
Quenching
Serum albumin
Spectra
Synchronous
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Summary:In this paper, glutathione (GSH) modified CdTe quantum dots (CdTeSH QDs) were synthesized in an aqueous solution. Then, the binding of the CdTeSH 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 CdTeSH 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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
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ObjectType-Feature-1
ISSN:0022-2313
DOI:10.1016/j.jlumin.2012.09.015