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目的研究金属离子对牛蒡子苷与牛血清白蛋白(bovine serum albumin,BSA)结合的影响。方法采用同步荧光光谱法,在拟生理pH条件下考察不同的金属离子(Cu2+、Mg2+、Zn2+)对牛蒡子苷与BSA结合作用的影响。结果在金属离子(Cu2+、Mg2+、Zn2+)存在下,随着体系中牛蒡子苷浓度增大,BSA荧光增强,两者间的结合力仍以静电作用力为主。金属离子存在时,牛蒡子苷与BSA的结合常数在25℃时,分别为7.899×104(无金属离子)、8.557×104(Cu2+)、6.724×104(Zn2+)、7.062×104(Mg2+);在37℃时,结合常数分别为5.962×104(无金属离子)、6.096×104(Cu2+)、5.915×104(Zn2+)、5.612×104(Mg2+)。结论金属离子的存在会影响牛蒡子苷与牛血清白蛋白的结合。Cu2+存在下,牛蒡子苷与BSA之间的结合常数增大;锌离子和镁离子存在下,两者的结合常数减小。
Objective To study the effect of metal ions on the binding of arctiin and bovine serum albumin (BSA). Methods Synchronous fluorescence spectroscopy was used to investigate the effects of different metal ions (Cu2 +, Mg2 +, Zn2 +) on the binding of arctiin and BSA at physiological pH. Results In the presence of metal ions (Cu2 +, Mg2 +, Zn2 +), BSA fluorescence increased with the concentration of arctiin in the system increased, and the binding force between the two still dominated by electrostatic force. In the presence of metal ions, the binding constants of arctiin and BSA were 7.899 × 104 (without metal ions), 8.557 × 104 (Cu2 +), 6.724 × 104 (Zn2 +) and 7.062 × 104 (Mg2 +) respectively at 25 ℃. At 37 ℃, the binding constants were 5.962 × 104 (without metal ions), 6.096 × 104 (Cu2 +), 5.915 × 104 (Zn2 +) and 5.612 × 104 (Mg2 +) respectively. Conclusion The existence of metal ions will affect the arctiin and bovine serum albumin binding. In the presence of Cu2 +, the binding constant between arctiin and BSA increased, while in the presence of zinc ions and magnesium ions, the binding constants decreased.