Binding nature and conformational alternations of bovine serum albumin upon interaction with synthesized LaF3:Ce,Tb luminescent nanocrystals using multi-spectroscopic approach

July 28, 2017

Title

Binding nature and conformational alternations of bovine serum albumin upon interaction with synthesized LaF3:Ce,Tb luminescent nanocrystals using multi-spectroscopic approach

Author

Xingjia Guo, Aijun Hao, Qiong Wu, Xin Diao, Wenjing Liu, Chenri Cong, Ye Sun, Liping Xu, Jie Yao

Year

2016

Journal

Journal of Luminescence

Abstract

Water-soluble LaF3:Ce,Tb luminescent nanocrystals (RLNCs) were successfully fabricated according to previously reported literatures. The experimental results indicate that the as-prepared nanocrystals consist of well crystallized hexagonal phases, having a nearly spherical shape with an average diameter of 10 nm. The interaction of RLNCs with bovine serum albumin (BSA) was studied mainly via fluorescence quenching in combination with circular dichroism (CD) and ultraviolet-visible (UV-vis) absorption spectroscopy under imitated physiological conditions. The fluorescence titration results reveal that RLNCs could efficiently quench the intrinsic fluorescence of BSA mainly through a dynamic quenching procedure. The binding constant and the number of binding site at 300 K were estimated to be 4.606×103 L mol−1 and 0.98, respectively. Meanwhile, the thermodynamic parameters for RLNCs-BSA system were also determined, suggesting that the binding reaction between RLNCs and BSA took place spontaneously and was primarily driven by hydrophobic forces. Furthermore, it was found that the binding of RLNCs to BSA was mainly located in site I and the binding distance was estimated to be 3.0 nm. Finally, the synchronous fluorescence, three dimensional (3D) fluorescence, and CD spectroscopy were used to explore the conformational alterations of protein induced by RLNCs.

Instrument

J-810

Keywords

Circular dichroism, Ligand binding, Nanostructures, Secondary structure, Biochemistry, Materials