Binding nature and conformational alternations of bovine serum albumin upon interaction with synthesized LaF3:Ce,Tb luminescent nanocrystals using multi-spectroscopic approach
Journal of Luminescence(2016)
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 10nm. 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 300K were estimated to be 4.606×103Lmol−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 3.0nm. Finally, the synchronous fluorescence, three dimensional (3D) fluorescence, and CD spectroscopy were used to explore the conformational alterations of protein induced by RLNCs.
MoreTranslated text
Key words
LaF3:Ce,Tb luminescent nanocrystals,Bovine serum albumin,Spectroscopic methods,Potential toxicity
AI Read Science
Must-Reading Tree
Example
![](https://originalfileserver.aminer.cn/sys/aminer/pubs/mrt_preview.jpeg)
Generate MRT to find the research sequence of this paper
Chat Paper
Summary is being generated by the instructions you defined