氮掺杂碳量子点与牛血清白蛋白相互作用的研究

Study on Interaction Between Nitrogen Doped Carbon Quantum Dots and Bovine Serum Albumin

采用光谱法研究了掺氮碳量子点(N-CQDs)与牛血清白蛋白(BSA)的相互作用机理。光谱分析表明,N-CQDs能有效猝灭BSA的内源性荧光,属于静态猝灭机制。N-CQDs的加入导致色氨酸残基微环境的疏水性降低,继而引起BSA的构象产生变化。N-CQDs与BSA可能是以1∶1的比例相互结合形成了稳定的复合物。结合热力学参数进行分析,N-CQDs与BSA相互结合的作用力主要为静电吸引力,反应为自发进行。同步荧光光谱也表明,N-CQDs与BSA的结合改变了BSA的构象。此研究数据可为进一步了解N-CQDs纳米颗粒在生物体内的应用提供参考。

The interaction mechanism between nitrogen doped carbon quantum dots(N-CQDs)and bovine serum albumin(BSA)was studied by spectroscopic method.Spectral analysis showed that N-CQDs could effectively quench the endogenous fluorescence of BSA,which belonged to the static quenching mechanism.The addition of N-CQDs resulted in a decrease in the hydrophobicity of the tryptophan residue microenvironment,which in turn caused a change in the conformation of BSA.N-CQDs and BSA may combine in a ratio of 1:1 to form a stable complex.According to the analysis of thermodynamic parameters,the binding force type of N-CQDs and BSA was mainly electrostatic force,and the reaction was spontaneous.Simultaneous fluorescence spectra also showed that the binding of N-CQDs with BSA changed the conformation of BSA.This research data provided a reference for the further understanding of N-CQDs nanoparticles in vivo applications.