摘要
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.
作者
李春兴
王芸
胡晓熙
余霭雯
沈俊尧
邱华
LI Chunxing;WANG Yun;HU Xiaoxi;YU Aiwen;SHEN Junyao;QIU Hua(Guangdong Songshan Polytechnic,Shaoguan 512126,China)
出处
《化工技术与开发》
CAS
2024年第5期26-30,共5页
Technology & Development of Chemical Industry
基金
2022年度广东松山职业技术学院校级科研项目(2022KJYB02)
2021年度广东松山职业技术学院校级科研项目(2021KJYB07)
2022年度广东省普通高校重点领域专项(2022ZDZX2075)
韶关市社会发展科技协同创新体系建设项目(220603164530591)。
关键词
氮掺杂碳量子点
牛血清白蛋白
光谱法
相互作用
nitrogen-doped carbon quantum dots
bovine serum albumin
spectroscopic method
interaction
