Fluorescence probe techniques to study the interaction between hydroxylated polybrominated diphenyl ethers (OH-PBDEs) and protein disulfide isomerase (PDI)

被引：3
作者：
He, Xiaoyan [1 ]
Zhang, Huimin [1 ]
Wu, Jun [1 ]
Qiu, Bin [1 ,2 ]
Lin, Zhenyu [1 ]
Chen, Guonan [1 ]
Cai, Zongwei [2 ]
机构：
[1] Fuzhou Univ, Fujian Prov Key Lab Anal & Detect Food Safety, Key Lab Anal & Detect Food Safety, Minist Educ, Fuzhou 350002, Fujian, Peoples R China
[2] Hong Kong Baptist Univ, Dept Chem, Hong Kong, Hong Kong, Peoples R China
来源：
ANALYTICAL METHODS | 2014年 / 6卷 / 20期
基金：
国家科技攻关计划;
关键词：
BROMINATED FLAME RETARDANTS; ANTI-CHAPERONE ACTIVITY; ENDOPLASMIC-RETICULUM; HORMONE-BINDING; IN-VITRO; CELLS; IDENTIFICATION; METABOLITES; REDUCTION; THYROXINE;
D O I：
10.1039/c4ay01134a
中图分类号：
O65 [分析化学];
学科分类号：
070302 ; 081704 ;
摘要：
A selective and sensitive method to study the interaction between hydroxylated polybrominated diphenyl ethers (OH-PBDEs) and protein disulfide isomerase (PDI) was established in this assay. In this report, 3,3',5-triiodo-thyronine (T3) was conjugated with fluorescein (FITC) as a fluorescence probe (F-T3) to study the competitive binding interaction of OH-PBDEs to PDI, which was observed to exhibit T3 binding activity. The findings suggest that some OH-PBDEs have the potential of binding to PDI, and they share the same binding site as T3 to PDI; moreover, OH-PBDEs were able to act as a competitive inhibitor in PDI binding to T3.
引用
收藏
页码：8106 / 8109
页数：4
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