期刊
FOOD AND CHEMICAL TOXICOLOGY
卷 49, 期 12, 页码 3158-3164出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.fct.2011.09.011
关键词
Sudan II; Sudan IV; Bovine serum albumin; Fluorescence quenching; UV-vis; Circular dichroism
资金
- NSFC [20875055]
- Ministry of Education of China [708058]
- Key Science-Technology Project in Shandong Province [2008GG10006012]
In this paper, we report the interaction of Sudan II and Sudan IV to bovine serum albumin (BSA). Structural analysis showed that both Sudan II and Sudan IV interact mainly with BSA at the hydrophobic pocket and via Van der Waals forces. The number of bound Sudan molecule for each protein molecule was approximately 1. The overall binding constants at 293 K (20 degrees C) estimated for Sudan II and Sudan IV were 1.22 x 10(4) M-1 and 1.48 x 10(4) M-1, respectively. BSA backbone structure was damaged by the dyes with more severe phenomenon observed for Sudan IV. For two Sudan dyes with the same concentration, Sudan IV could cause more alterations on CD spectra of BSA with slight decrease of alpha-helical content and increase of beta-sheet content, suggesting a partial protein unfolding. (C) 2011 Elsevier Ltd. 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