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机构地区:[1]南昌大学化学系,江西南昌330031 [2]南昌大学食品科学与技术国家重点实验室,江西南昌330047
出 处:《南昌大学学报(理科版)》2009年第3期244-248,共5页Journal of Nanchang University(Natural Science)
基 金:国家自然科学基金资助项目(20562009);江西省自然科学基金资助项目(0620041);中科院长春应化所电分析化学重点实验室项目(SKLEAC2004-3);长江学者及创新团队项目(IRT0540)
摘 要:应用荧光光谱法和紫外-可见吸收光谱法研究了金霉素(CTC)和土霉素(OTC)与牛血清白蛋白(BSA)之间的相互作用。发现在pH=7.4的三羟甲基胺基甲烷-盐酸缓冲溶液(Tris-HCl)中,随着金霉素或土霉素浓度的增加BSA的荧光强度逐渐减弱,说明它们之间的作用为荧光猝灭作用。求得金霉素与BSA的结合常数为K=1.36×105M-1(T=300 K)和K=1.20×105M-1(T=310 K),而土霉素的结合常数为K=1.69×105M-1(T=300K)和K=1.43×105M-1(T=310 K)。依据Forster非辐射能量转移理论确定了授体-受体间的结合距离分别为2.23 nm和2.11 nm;并根据热力学参数确定了药物与牛血清白蛋白之间的作用力类型为静电引力。本工作还采用同步荧光光谱法研究了金霉素和土霉素对BSA构象的影响。The interaction between tetracyclines ( chlorotetracycline (CTC) and oxytetracyline ( OTC ) ) and bovine serum albumin (BSA) was investigated by fluorescence and UV - vis spectroscopy. The influence of some metal ions on the interaction wre also studied. When tetracycline were added into the solution containing BSA,the fluorescence intensity of BSA decreased with the increasing of the drug concentrations, indicating their interactions were involving fluorescence quenching. The Stern - Volmer quenching constant Ksv, binding constant K and corresponding thermodynamic parameters AH,AG, and AS were calculated. The main sorts of acting force between the drug and BSA were found to be electrostatic force. The distances, r, between donor (BSA) and acceptor (CTC and OTC ) were calculated according to fluorescence resonance energy transfer (FRET).
关 键 词:金霉素 土霉素 牛血清白蛋白 荧光光谱法 紫外-可见吸收光谱法
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