Optical, structural and thermodynamic properties of the interaction between tradimefon and serum albumin

Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy
Hua-xin ZhangXi-Xiong Yang

Abstract

The biological toxicity of a chloric pesticide, tradimefon to bovine serum albumin (BSA) were studied by fluorescence and absorption spectroscopy. The fluorescence quenching mechanism analysis indicates the quenching of BSA by TDF was caused by BSA-TDF complex formation and electrostatic interaction played major role in the reaction. The number of binding sites n and observed binding constant K(b) was measured by fluorescence quenching method. The thermodynamic parameters DeltaH(theta), DeltaG(theta), DeltaS(theta) at different temperatures were calculated, and the distance r between donor (BSA) and acceptor (TDF) was obtained according to Förster theory of non-radiation energy transfer. Three-dimensional fluorescence spectra, circular dichroism (CD) spectra and synchronous fluorescence spectra were used to investigate the structural change of BSA molecules with addition of TDF and the mechanism of binding reaction was analyzed at molecular level.

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Citations

Nov 30, 2010·Biological Trace Element Research·Hua-xin Zhang, Ping Mei
Jul 27, 2011·Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy·Ling-Ling HeShu-Kun Xu
Feb 27, 2014·Food and Chemical Toxicology : an International Journal Published for the British Industrial Biological Research Association·Sheying DongTinglin Huang
Apr 16, 2010·Analytical and Bioanalytical Chemistry·Srabanti GhoshAbhijit Saha
Feb 10, 2012·Molecular Biology Reports·Hua-xin Zhang, Zhen-xia Huang
Jun 15, 2011·Molecular Biology Reports·Hua-xin Zhang, Lin Liu
Sep 8, 2021·Luminescence : the Journal of Biological and Chemical Luminescence·Guo Fei ZhuWang Wang

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