论文部分内容阅读
应用荧光光谱法研究了4种金属卟啉配合物5-(4-羧基苯基)-10,15,20-三苯基卟啉锌、钴、镍、锰(MCPPZn、MCPP-Co、MCPPNi、MCPPMnCl)与牛血清白蛋白(BSA)的结合反应。探讨了金属卟啉配合物对BSA内源荧光的猝灭机理,根据不同温度下的结合常数判断金属卟啉配合物与BSA之间具有较强的结合作用,对BSA内源荧光的猝灭过程为静态猝灭。根据热力学参数确定了MCPPZn与BSA之间的作用力以静电引力为主,MCPPCo(25和42℃下)、MCPPNi、MCP-PMnCl与BSA之间的作用力以氢键和范德华力为主。分析了结合常数和作用力类型的差异主要是由中心金属离子的电负性和外层d轨道上的电子数的不同而引起的。
Fluorescence spectroscopy was used to study the effects of four metalloporphyrin complexes, such as zinc (5- (4-carboxyphenyl) -10,15,20-triphenylporphyrin, cobalt, nickel and manganese (MCPPZn, MCPP-Co, MCPPNi, MCPPMnCl) with bovine serum albumin (BSA). The quenching mechanism of endogenous fluorescence of BSA by metalloporphyrin complexes was explored. According to the binding constants at different temperatures, the binding of metalloporphyrin complexes to BSA was stronger and the endogenous fluorescence quenching process of BSA Quenching for static. Based on the thermodynamic parameters, the interaction between MCPPZn and BSA is dominated by electrostatic attraction. The interaction between MCPPCo (at 25 and 42 ℃), MCPPNi, MCP-PMnCl and BSA is dominated by hydrogen bonding and van der Waals forces. It is analyzed that the difference between the binding constants and the type of force is mainly caused by the difference between the electronegativity of the central metal ion and the number of electrons in the outer d orbit.