CAJ | 학술논문

利用荧光光谱和吸收光谱研究了贝加因与牛血清白蛋白(BSA)的相互作用,由Van't Hoff方程计算了反应的热力学参数,并根据Stern-Volmer方程计算了不同温度下的结合位点和结合常数.结果表明,贝加因可静态猝灭BSA的内源荧光;二者相互作用的焓变和熵变均大于零,说明疏水作用力是二者之间的主要作用力.与此同时,贝加因可诱导牛血清白蛋白构象变化.相关研究结果有助于在分子水平上更好地理解药物的作用机理以及吸收和分布特性.
이용형광광보화흡수광보연구료패가인여우혈청백단백(BSA)적상호작용,유Van't Hoff방정계산료반응적열역학삼수,병근거Stern-Volmer방정계산료불동온도하적결합위점화결합상수.결과표명,패가인가정태졸멸BSA적내원형광;이자상호작용적함변화적변균대우령,설명소수작용력시이자지간적주요작용력.여차동시,패가인가유도우혈청백단백구상변화.상관연구결과유조우재분자수평상경호지리해약물적작용궤리이급흡수화분포특성.
The interaction between baicalein and bovine serum albumin(BSA)was studied by means of fluorescence spectrometry and absorption spectrometry. The thermodynamic parameters of the reaction were calculated using Van't Hoff equation. Besides, the number of binding sites and the apparent binding constants at different temperatures were calculated from fluorescence quenching data using Stern-Volmer equation. Results indicate that baicalein is able to quench the intrinsic fluorescence of BSA via static quenching mechanism. The changes of enthalpy and entropy for the reaction of baicalein and BSA are both above 0, which indicates that their interaction is dominated by intermolecular hydrophobic force. Moreover, baicalein is able to induce the conformational change of BSA. Relevant results could help to better understand the action mechanism as well as absorption and distribution features of drugs at molecular level.