醋酸可的松及其代谢物与牛血清白蛋白相互作用机制的研究  

Study on the Interaction Mechanism of Cortisone Acetate and Its Metabolite with Bovine Serum Albumin

作　　者：顾佳丽[1] 刘璐[1] 黄曦瑶 何茜 李响 GU Jia-li;LIU Lu;HUANG Xi-yao;HE Qian;LI Xiang(College of Chemistry and Materials Engineering,Bohai University,Jinzhou 121013,China;Shenyang Photosensitive Chemical Research Institute Co.,Ltd.,Shenyang 110141,China)

机构地区：[1]渤海大学化学与材料工程学院,辽宁锦州121013 [2]沈阳感光化工研究院有限公司,辽宁沈阳110141

出　　处：《化学试剂》2021年第6期820-824,共5页Chemical Reagents

基　　金：国家自然科学基金资助项目(41602351)。

摘　　要：采用荧光光谱法和紫外-可见吸收光谱法研究了醋酸可的松(CA)及其代谢产物氢化可的松(HS)与牛血清白蛋白(BSA)之间的作用机理。实验结果表明,CA和HS均通过疏水作用与BSA形成复合物,其结合常数分别为2.04×10^(4) L/mol和2.02×10^(3) L/mol。CA/HS对氨基酸残基周围的微环境没有显著影响。HS会使CA与BSA作用的结合常数减小,结合距离增大,但没有改变其主要作用力类型。The interaction mechanism between cortisone acetate(CA)and its metabolite hydrocortisone(HS)with bovine serum albumin(BSA)were studied by fluorescence spectroscopy and UV-Vis absorption spectroscopy.The results showed that CA and HS formed complex with BSA through hydrophobic interaction,and their binding constants were 2.04×104 L/mol and 2.02×103 L/mol,respectively.The micro-environment around the amino acid residues engaged no significant change in the present of CA/HS.As shown,the HS decreases the binding constant and increases the binding distance for the CA-BSA interaction,but does not change its main force type.

关 键 词：醋酸可的松 氢化可的松 牛血清白蛋白 相互作用 

分 类 号：O657[理学—分析化学]