Investigation on the interaction between ilaprazole and bovine serum albumin without or with different C-ring flavonoids from the viewpoint of food-drug interference.

Investigation on the interaction between ilaprazole and bovine serum albumin without or with different C-ring flavonoids from the viewpoint of food-drug interference.
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DOI:
10.1021/jf201796x
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发表时间:
2011-07
影响因子:
6.1
通讯作者:
Yuping Zhang;S. Shi;Xiaoqing Chen;Wei Zhang;Ke‐long Huang;Mijun Peng
Yuping Zhang;S. Shi;Xiaoqing Chen;Wei Zhang;Ke‐long Huang;Mijun Peng
中科院分区:
农林科学1区
文献类型:
--
作者:
Yuping Zhang;S. Shi;Xiaoqing Chen;Wei Zhang;Ke‐long Huang;Mijun Peng

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采用荧光光谱法研究了艾普拉唑与牛血清白蛋白(BSA)在槲皮素、木犀草素、紫杉叶素和(+)-儿茶素四种不同C环结构黄酮类化合物存在和不存在的情况下的相互作用。结果表明,艾普拉唑对BSA的内源荧光有较强的猝灭作用,位点标记竞争实验表明艾普拉唑与BSA的结合主要发生在IIA亚结构域。黄酮类化合物对BSA的荧光猝灭过程有明显的影响,但并不改变BSA对艾普拉唑的猝灭机制,而是通过静态猝灭和非辐射能量转移相结合的方式进行猝灭。黄酮类化合物的存在使艾普拉唑与BSA的猝灭常数从2.2%降低到23.7%,结合常数从73.7%降低到98.3%,这取决于黄酮类化合物的不同结构。槲皮素、木犀草素和紫杉叶素的引入降低了艾普拉唑与BSA的结合常数,但空间距离不变,这可能是由于黄酮类化合物和艾普拉唑与BSA竞争结合所致;而(+)-儿茶素的引入降低了艾普拉唑与BSA的结合常数,但空间距离增加,这可能是由于艾普拉唑与BSA-(+)-儿茶素形成三元复合物所致。所有这些结果可能有相关的后果合理化的干扰,常见的食物胃溃疡的治疗。
The interaction between ilaprazole and bovine serum albumin (BSA) has been investigated in the absence and presence of four popular flavonoids with different C-ring structures, quercetin, luteolin, taxifolin, and (+)-catechin, by means of fluorescence spectroscopy. The results indicated that ilaprazole had a strong ability to quench the intrinsic fluorescence of BSA, and site marker competitive experiments indicated that the binding of ilaprazole to BSA primarily took place in subdomain IIA. The quenching process of ilaprazole with BSA was easily affected by flavonoids,; however, they did not change the quchenching mechanism of ilaprazole with BSA, whereas all of the fluorescence quenching was initiated by a static quenching procedure combining with nonradiative energy transfer. The presence of flavonoids decreased the quenching constants of ilaprazole with BSA from 2.2 to 23.7% and decreased the binding constants from 73.7 to 98.3%, which depended on the different flavonoids' structures. The decreased binding constants and unchangeable spatial distance of ilaprazole with BSA by the introduction of quercetin, luteolin, and taxifolin may result from the competition of flavonoids and ilaprazole binding to BSA, whereas in the presence of (+)-catichin, decreased binding constants and increased spatial distance possibly resulted from the formation of a ternary ilaprazole-BSA-(+)-catechin complex. All of these results may have relevant consequences in rationalizing the interferences of common food to gastric ulcer treatments.