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Thermodynamic and conformational investigation of the influence of CdTe QDs size on the toxic interaction with BSA
Authors:Qisui Wang  Pengfei LiuXiaolan Zhou  Xiaolei ZhangTingting Fang  Peng Liu  Xinmin Min  Xi Li
Institution:a Department of Chemistry, School of Sciences, Wuhan University of Technology, Wuhan 430070, PR China
b State Key Laboratory of Advanced Technology for Materials Synthesis and Processing, School of Materials Science and Engineering, Wuhan University of Technology, Wuhan 430070, PR China
c Department of Electronic Engineering, Artillery Academy of PLA, Hefei Artillery Academy of PLA, Hefei 230031, PR China
d Institute of High Pressure and Temperature Physics, School of Sciences, Wuhan University of Technology, Wuhan 430070, PR China
Abstract:Water-soluble fluorescent colloidal quantum dots (QDs) have been widely used in some biological and biomedical fields, so the interaction of QDs with biomolecules recently attracts increasing attention. In this study, the fluorescence (FL) quenching method, circular dichroism (CD) technique, attenuated total reflection-Fourier transform infrared (ATR-FTIR) and UV-vis absorption spectra were used to investigate systematically the influence of CdTe QDs size on the toxic interaction with bovine serum albumin (BSA). Three size CdTe QDs with maximum emission of 543 nm (green-emitting QDs, GQDs), 579 nm (yellow-emitting QDs, YQDs) and 647 nm (red-emitting QDs, RQDs) were tested. The Stern-Volmer quenching constant (Ksv) at different temperatures, corresponding thermodynamic parameters (ΔH, ΔG and ΔS), and information of the structural features of BSA were gained. The FL results indicated that QDs can effectively quench the FL of BSA in a size-dependent manner, electrostatic interactions play a major role in the binding reaction, and the nature of quenching is static, resulting in forming QDs-BSA complexes. The CD and ATR-FTIR spectra showed that the secondary structure of BSA was changed by QDs, indicating the toxic on protein.
Keywords:Quantum dot  BSA  Size  Thermodynamic parameter  Conformational change
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