摘要
The interaction between bovine serum albumin(BSA) and five active components of Chinese Herb CⅠ-CⅤ containing structural unit of coumarin was investigated by ultraviolet(UV) and fluorescence spectroscopy(FS).The intrinsic fluorescence of BSA was quenched by pharmaceuticals via forming pharmaceutical-BSA complexes.The quenching mechanism is mainly a combination of static quenching with nonradiative energy transfer.The parameters of pharmaceutical-BSA binding process,such as statistic quenching constant K_P,the apparent association constant K_A,the value of binding site n,the efficiency of energy transfer E,the spatial distance r and ΔG were obtained.The above parameters disclose the structural-performance relationship of pharmaceutical-BSA interaction as follows.The process of pharmaceutical-BSA binding is promoted strongly by both 4-methyl and 6-hydroxyl in coumarin molecule,but the latter must endure simultaneously some(adverse) effects caused by increment of molecular polarity and stereo hindrance.Decreasing the polarity of(7-substituent) group and increasing the volume of substituting group destroys the pharmaceutical-BSA binding,and the effect is almost totally opposite to that of 6-hydroxyl.
The interaction between bovine serum albumin（BSA） and five active components of Chinese Herb C Ⅰ-CⅤ containing structural unit of coumarin was investigated by ultraviolet（UV） and fluorescence spectroscopy（FS）. The intrinsic fluorescence of BSA was quenched by pharmaceuticals via forming pharmaceutical-BSA complexes. The quenching mechanism is mainly a combination of static quenching with nonradiative energy transfer. The parameters of pharmaceutical-BSA binding process, such as statistic quenching constant KP, the apparent association constant KA, the value of binding site n, the efficiency of energy transfer E, the spatial distance r and AG were obtained. The above parameters disclose the structural-performance relationship of pharmaceutical-BSA interaction as follows. The process of pharmaceutical-BSA binding is promoted strongly by both 4-methyl and 6-hydroxyl in coumarin molecule, but the latter must endure simultaneously some adverse effects caused by increment of molecular polarity and stereo hindrance. Decreasing the polarity of 7-substituent group and increasing the volume of substituting group destroys the pharmaceutical-BSA binding, and the effect is almost totally opposite to that of 6-hydroxyl.
出处
《高等学校化学学报》
SCIE
EI
CAS
CSCD
北大核心
2006年第1期150-152,共3页
Chemical Journal of Chinese Universities
基金
江南大学自然科学预研基金(批准号:2004LYY019)资助
关键词
构效关系
中药
香豆素
牛血清白蛋白
荧光光谱
Structural-performance relationship
Chinese Herb
Coumarin
Bovine serum albumin
Fluorescence spectroscopy
