摘要
在模拟人体生理条件下,采用多种光谱法研究了牛血清白蛋白(BSA)与利培酮(RI)猝灭反应的信息.研究表明:加入RI后,通过动态猝灭机制,BSA的荧光强度明显下降.通过计算得出RI与BSA的速率常数(Kq)、猝灭常数(Ksv)、结合位点数(n)、结合常数(Kc)和Hill系数(nH).使用范托夫方程测定热力学参数、焓变化(ΔH),熵变(ΔS)和吉布斯自由能(ΔG).结果表明,RI与BSA的相互作用是自发的.静电作用力是主要的作用力类型.同步荧光光谱表明结合位点更接近于色氨酸,RI对BSA构象产生一定的影响.RI与BSA的结合位点主要位于BSA的亚螺旋域ⅡA中.nH≈1,表明RI分子之间对结合反应几乎无协同作用.同时还探讨了共存金属离子对RI与BSA结合作用的影响.
Under the simulation of the human body physiological conditions,the information of the quenching reaction of bovine serum albumin（BSA）with risperidone（RI）is obtained by multi-spectroscopic methods.The results of fluorescence spectroscopy indicated that the fluorescence intensity of BSA was decreased considerably upon the addition of RI through a dynamic quenching mechanism.The rate constant（Kq）,quenching constant（Ksv）,binding constants（Kc）,the corresponding number of binding sites and Hill’s coefficients（nH）were obtained by calculation.The thermodynamic parameters including enthalpy change（ΔH）,entropy change（ΔS）and also Gibb’s free energy（ΔG）were determined using Van’t Hoff equation.These values showed that the interaction of RI and BSA was spontaneous.Also,hydrophobic force was the main interactions in the binding of RI to BSA.Studies utilizing synchronous spectra showed that the binding site of RI and BSA was near by tryptophan residue and the conjugation reaction between RI and BSA would affect the conformation of BSA.Moreover,it was recognized that RI binds within the sub-domain IIA pocket in domain II of BSA.The values of nH were nearly 1,which indicated that there was nearly no cooperative effect.In addition,the effect of metal ions on the binding constant of RI with BSA was also studied.
出处
《河北师范大学学报（自然科学版）》
CAS
2016年第4期320-325,共6页
Journal of Hebei Normal University：Natural Science
基金
国家自然科学基金(21261019)
云南省教育科学研究基金(2015C090Y)
