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作 者:刘萍 郭嘉鑫 刘中天 LIU Ping;GUO Jia-xin;LIU Zhong-tian(College of Chemical Engineering and Modern Materials/Shaanxi Key Laboratory of Comprehensive Utilization of Tailings Resources/Shaanxi Engineering Research Center for Mineral Resources Clean&Efficient Conversion and New Materials,Shangluo University,Shangluo726000,Shaanxi)
机构地区:[1]商洛学院化学工程与现代材料学院/陕西省尾矿资源综合利用重点实验室/陕西省矿产资源清洁高效转化与新材料工程研究中心,陕西商洛726000
出 处:《商洛学院学报》2023年第6期57-62,共6页Journal of Shangluo University
基 金:陕西省大学生创新创业训练计划项目(S202311396074);商洛学院无机化学线下一流课程建设项目(2020ylkc014)。
摘 要:以Tris-HCl溶液为缓冲溶液,运用紫外可见吸收光谱法研究了中药小分子红花黄色素与牛血清蛋白(BSA)的相互作用情况,测试了283 K和310 K时的结合常数,考查了共存金属离子Cu^(2+)、Ni^(2+)、Zn^(2+)对二者结合常数的影响,计算了它们结合过程的ΔG、ΔH、ΔS。同时采用荧光光谱法测定了红花黄色素对BSA的荧光猝灭类型及二者的结合常数和结合位点数。结果表明,红花黄色素与BSA的结合常数随着温度的升高有不同程度的降低,其结合过程是一个焓和熵共同驱动的自发过程,二者之间的作用力主要表现为静电引力。此外,金属离子Cu^(2+)、Ni^(2+)、Zn^(2+)的存在降低了红花黄色素与BSA的结合常数,表明金属离子与红花黄素之间存在着竞争效应。The interactions between saffron yellow pigment and bovine serum albumin(BSA)were studied by UV-vis absorption spectroscopy using Tris-HCl solution as a buffer.The binding constants at 283 K and 310 K were tested,and the effects of coexisting metal ions Cu^(2+),Ni^(2+),and Zn^(2+)on the binding constants were investigated.ΔG,ΔH andΔS of the process were calculated.At the same time,the fluorescence quenching type of safflower yellow pigment on BSA,as well as the binding constant and number of binding sites were determined by fluorescence spectroscopy.The results indicated that the binding constant between safflower yellow pigment and BSA decreased with the temperature increasing.The binding process is a spontaneous process driven by both enthalpy and entropy,and the main force between the two is electrostatic attraction.In addition,the binding constant between safflower yellow pigment and BSA was decreased with the presence of metal ions Cu^(2+),Ni^(2+),and Zn^(2+),indicating competition between metal ions and safflower yellow pigment.
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