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作 者:滕晓鹏 任婷 恽鸿博 时建伟[2] 滕晓旭[2] 曹团武[2] TENG Xiao-peng;REN Ting;YUN Hong-bo;SHI Jian-wei;TENG Xiao-xu;CAO Tuan-wu(Xing'an League People’s Hospital Urology,Inner Mongolia Autonomous Region,Ulan Hot 137400,China;Laboratory of Natural Medicine Research and Development in Wuling Mountain,School of Chemistry and Chemical Engineering,Yangtze Normal University,Chongqi Fuling 408100,China)
机构地区:[1]兴安盟人民医院,内蒙古自治区乌兰浩特137400 [2]长江师范学院化学化工学院,武陵山天然药物研究与开发实验室,重庆涪陵408100
出 处:《化学研究与应用》2021年第11期2179-2185,共7页Chemical Research and Application
基 金:国家自然科学基金项目(21808017)资助。
摘 要:利用光谱法在不同温度和模拟生理pH条件下,研究了比克白芷素(Byakangelicin,BYA)与人血清白蛋白(human serum albumin,HSA)之间的作用机制。结果表明,在不同温度下,通过静态猝灭机制,BYA使HSA内源荧光发生有规律的猝灭,两者的结合常数K_(a)>1×10^(4) mol·L^(-1),结合位点数n接近于1。BYA与HSA相互作用的热力学参数△G<0、△H>0、△S>0,表明BYA与HSA的结合过程是自发进行的,主要作用力是疏水作用力。由Förester非辐射转移理论计算出不同条件下BYA与HSA的结合距离r为2.95~3.20 nm。BYA使HSA的色氨酸和酪氨酸残基所处的微环境极性增强、疏水性减弱导致HSA肽链结构发生了改变。The interaction mechanism between Byakangelicin(BYA)and human serum albumin(HSA)was studied by spectroscopic methods under different temperature and simulated physiological pH.The results showed that the intrinsic fluorescence of HSA was regularly quenched by BYA through static quenching mechanism.At different temperatures,all the magnitude of binding constants(K_(a))were larger than 10^(4) L·mol^(-1) and the number of binding sites(n)in the binary system were approximate to 1.The enthalpy change(△H)and entropy change(△S)were greater than 0,which implied that the main interaction force of BYA with HSA was hydrophobic force.The negative values of energy(△G)showed that was spontaneous and exthermic process.The binding distance(r)between the BYA and HSA were calculated to be from 2.95 nm to 3.20 nm by the F?rster’s non-radiation energy transfer theory,which indicated that the energy transfer from HSA to BYA occurs having strong possibility.The conformation of HSA was changed during the binding reaction of BYA with HSA through the synchronous and 3D florescence spectroscopy.
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