摘要
应用荧光光谱、紫外吸收光谱和核磁共振波谱研究了5,7-二羟基-4'-甲氧基二氢黄酮(ISO)与牛血清白蛋白(BSA)分子间的相互作用.研究表明:ISO对BSA内源性荧光的猝灭机制属于ISO和BSA形成化合物所引起的静态猝灭;二者的结合常数为7.41×1011L/mol,结合位点数为1.98.ISO与BSA作用的活性部位为其分子内的7-OH和5-OH,且7-OH活性强于5-OH,并且随着ISO浓度增大,BSA的构象发生了变化.
The interaction between 5,7-dihydroxy-4′-methoxyflavanone （isosakuranetin, ISO） and bovine serum albumin isosakuranetin （BSA） has been investigated by fluorescence, UV absorption spectra and NMR spectroscopy. The results show that the mechanism of quenching the inner fluorescence of BSA is due to the combination of BSA with ISO which results in static quenching procedure. The binding constant is 7.41 ^- 10^11L/mol and the number of binding sites is 1.98. The active groups of ISO interacting with BSA are 7-OH and 5-OH, and 7-OH is more active than 5-OH. With the increase of ISO concentration, the conformation of BSA has been changed.
出处
《化学学报》
SCIE
CAS
CSCD
北大核心
2006年第13期1361-1366,共6页
Acta Chimica Sinica
基金
河南省杰出青年科学基金(No.0612001100)资助项目.
