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采用荧光光谱法和紫外可见光谱法研究了硫唑嘌呤(AZP)和巯嘌呤(6-MP)与牛血清白蛋白(BSA)的结合反应特性。测定了不同温度下的结合常数KA及结合位点数n,研究证明AZP和6-MP对BSA内源荧光的猝灭机理均为静态猝灭,且主要以疏水作用力与BSA作用;利用同步荧光技术发现AZP和6-MP对BSA的构象均有影响;AZP和6-MP与BSA摩尔比为1∶1时,根据F rster偶极-偶极非辐射能量转移理论,计算出作用距离rAZP=2.94,r6-MP=4.10,说明AZP和6-MP与BSA的猝灭过程中都存在能量转移效应。
The binding properties of azathioprine (AZP) and mercaptopurine (6-MP) to bovine serum albumin (BSA) were studied by fluorescence spectroscopy and UV-vis spectroscopy. The binding constants KA and the number of binding sites n at different temperatures were measured. The quenching mechanisms of endogenous fluorescence of BSA by AZP and 6-MP were statically quenched, and the interaction between BSA and BSA was mainly attributed to hydrophobic interaction. Synchronous fluorescence The results show that both AZP and 6-MP have an effect on the conformation of BSA. When AZP, 6-MP and BSA molar ratio is 1: 1, according to F rster dipole-dipole non-radiative energy transfer theory, 2.94 and r6-MP = 4.10, indicating that there are energy transfer effects in the quenching of AZP, 6-MP and BSA.