期刊
EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY
卷 93, 期 -, 页码 492-500出版社
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.ejmech.2015.02.025
关键词
Loureirin A; Cochinchinenin C; Human serum albumin; Fluorescence quenching; Molecular docking
资金
- National Key Technology Support Program of China [2013BAD12B06]
The interactions of loureirin A (LA) and cochinchinenin C (CC) with human serum albumin (HSA) under simulated physiological conditions (pH = 7.4) have been studied with fluorescence, UV-vis absorption spectroscopic method and molecular docking technique. The results indicated that there was a synergistic interaction between LA and CC, and the fluorescence quenching of HSA by LA (or CC) was a combined quenching procedure (dynamic and static quenching). At low compound concentrations, the quenching constants K-SV of CC was larger than that of LA, which meant the CC efficacy may be better than that of LA. The negative Delta H and Delta S values suggested hydrogen bonds and van der Waals forces played the major role in the binding of LA (or CC) to HSA. The efficiency of energy transfer and distance between the compounds and HSA was calculated. Moreover, the results of synchronous and three-dimensional fluorescence demonstrated that the HSA microenvironment was changed in the presence of LA (or CC). Finally, the binding of LA (or CC) to HSA was modeled by molecular docking, which is in good accordance with the experimental studies. (C) 2015 Elsevier Masson SAS. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据