摘要
采用光谱法研究雷公藤红素(CSL)与牛血清白蛋白(BSA)的结合反应。实验表明:雷公藤红素对BSA的荧光猝灭为静态猝灭。二者之间的作用力为疏水作用力。在溶液中二者以摩尔比1:1结合,并求出二者的结合反应平衡常数。以华法林(Warfarin)和布洛芬(Ibuprofen)为标记物,采用竞争结合实验,利用紫外可见光谱法确定了雷公藤红素在BSA的结合位置为SiteI。根据Forster非辐射能量转移理论,求出了给体(BSA)与受体(CSL)间距离(r0)为2.31nm。另外,利用同步荧光法考察了雷公藤红素对牛血清白蛋白构象的影响。..
Fluorescent and UV-vis spectroscopic methods were adopted to study the binding reaction of celastrol （CSL） with bovine serum albumin （BSA）. The quenching of BSA by CSL was found to a static process. The primary binding pattern between celastrol and BSA was interpreted as hydrophobic interaction with the binding ratio of 1：1 under physiological conditions. It was found that celastrol was located near the Tyr residue region of site I in BSA by competitive binding experiments using warfarin and ibuprofen as site mariners. The distance between the donor （BSA） and receptor （celastrol）, r, was calculated to be 2.31 nm according to Frster＇s non-radiative energy transfer theory. In addition, the effect of celastrol on the conformation of BSA was analyzed using synchronous fluorescence spectroscopy.
出处
《食品科学》
EI
CAS
CSCD
北大核心
2009年第17期130-133,共4页
Food Science
基金
山东省自然科学基金项目(Y2006C107)
