掺氮碳量子点与牛血清白蛋白相互作用机制研究  

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

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)

机构地区：[1]广东松山职业技术学院,广东韶关512126

出　　处：《河南化工》2024年第8期1-4,9,共5页Henan 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(生物医药与健康)(2022ZDZX2075);韶关市社会发展科技协同创新体系建设项目(220603164530591)。

摘　　要：当碳纳米材料进入生物体的血液中时,与血浆中的血清白蛋白相互作用可能会导致蛋白质的构象改变,从而影响其生物活性。利用荧光光谱、紫外吸收光谱、三维荧光光谱法研究掺氮碳量子点(N-CQDs)与牛血清白蛋白(BSA)的相互作用机制。结果表明,N-CQDs能够有效猝灭BSA内部荧光,符合静态猝灭机制。N-CQDs与BSA能够自发性结合,其结合作用力主要是静电吸引力。N-CQDs的加入导致色氨酸和酪氨酸残基微环境发生变化,继而改变了BSA的分子构象。该研究可为N-CQDs在体内的进一步应用提供参考依据。When carbon nanomaterials enter the blood of organisms,their interaction with serum albumin in plasma may lead to conformational changes of proteins and affect their biological activities.The interaction mechanism between nitrogen-doped carbon quantum dots(N-CQDs)and bovine serum albumin(BSA)is studied by fluorescence,ultraviolet absorption and three-dimensional fluorescence spectroscopy.The results show that N-CQDs can effectively quench the endogenous fluorescence of BSA,which belongs to the static quenching mechanism.The binding force type of N-CQDs and BSA is mainly electrostatic attraction,and the reaction is a spontaneous process.The addition of N-CQDs led to changes in the microenvironment of tyrosine and tryptophan residues,which in turn caused conformational changes in BSA.This study can provide reference for the further application of N-CQDs in vivo.

关 键 词：掺氮碳量子点 牛血清白蛋白 相互作用 

分 类 号：TB383[一般工业技术—材料科学与工程] TQ936[化学工程]