摘要
目的研究吡罗昔康(PRCX)与人血白蛋白(HSA)的结合性质。方法采用荧光淬灭技术研究吡罗昔康对人血白蛋白内源荧光淬灭的类型,依据非辐射能量转移理论计算二者之间的结合距离,通过计算热力学参数确定二者相互作用的作用力类型,采用同步荧光和圆二色光谱研究蛋白质的构象变化。结果吡罗昔康能淬灭人血白蛋白的内源荧光,二者的结合距离小于7 nm,吡罗昔康与人血白蛋白相互作用的ΔG^0<0、ΔS^0>0、ΔH^0<0,吡罗昔康的加入导致人血白蛋白的同步荧光和圆二色光谱发生改变。结论吡罗昔康对人血白蛋白的荧光淬灭是静态淬灭,人血白蛋白与吡罗昔康之间能够发生非辐射能量转移,疏水作用力和氢键在形成人血白蛋白-吡罗昔康复合物的过程中发挥主要作用且形成复合物的过程是自发进行的,相互作用导致人血白蛋白的构象发生了变化。
Objective To study the binding characteristics of piroxicam（PRCX） to human serum albumin（HSA）.Methods The fluorescence quenching technology was used to study the fluorescence quenching type of HSA induced by PRCX.The binding distance of PRCX and the tryptophan residues of HSA was calculated according to the non-radiative energy transfer theory.The interaction force types of the interaction between HSA and PRCX were determined by the calculated results of thermodynamics parameters.The synchronous fluorescence and circular dichroism spectra were used to study the conformational changes of protein. Results The intrinsic fluorescence of HSA was quenched remarkably by PRCX. The value of the binding distance of PRCX and the tryptophan residues of HSA was less than 7 nm. The ΔG^0 was negative,the ΔS^0 was positive and the ΔH^0 was negative in the interaction between PRCX and HSA.The synchronous fluorescence and circular dichroism spectra of HSA change in the presence of PRCX.Conclusion The fluorescence quenching of HSA induced by PRCX was static quenching.The energy transfer from HSA to PRCX may occur.The formation processes of HSA-PRCX complex was spontaneous and both hydrophobic interactions and hydrogen bonding played major roles in the formation of HSA-PRCX complex.The interaction between PRCX and HSA can give rise to the changes of HSA conformation.
出处
《药学研究》
CAS
2018年第1期19-22,40,共5页
Journal of Pharmaceutical Research
基金
国家自然科学基金资助项目(No.21402125)
辽宁大学"大学生创新创业训练计划"项目(No.x201710140291)
关键词
光谱法
吡罗昔康
人血白蛋白
结合性质
Spectroscopic method
Piroxicam
Human serum albumin
Binding characteristic
