Study the interaction between CdTe@glutathione and human serum albumin

被引：12

作者：

Yang, Qing ^{[1
,2
]}

Zhou, Xi-min ^{[1
,2
]}

Zhu, Yi-shuo ^{[1
,2
]}

Chen, Xing-guo ^{[1
,2
]}

机构：

[1] Lanzhou Univ, Natl Key Lab Appl Organ Chem, Lanzhou 730000, Peoples R China

[2] Lanzhou Univ, Dept Chem, Lanzhou 730000, Peoples R China

来源：

JOURNAL OF LUMINESCENCE | 2013年 / 135卷

基金：

中国国家自然科学基金;

关键词：

CdTe@GSH QDs; Human serum albumin (HSA); Fluorescence spectroscopy; QUANTUM DOTS; IN-VITRO; FLUORESCENCE; NANOCRYSTALS; BINDING; CELLS; SPECTROSCOPY; CDSE;

D O I：

10.1016/j.jlumin.2012.09.015

中图分类号：

O43 [光学];

学科分类号：

070207 ; 0803 ;

摘要：

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 Os was confirmed by synchronous fluorescence spectra. (c) 2012 Elsevier B.V. All rights reserved.

引用

页码：335 / 338

页数：4

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