Issue 20, 2014
From the journal:

Analytical Methods

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

Xiaoyan He,a   Huimin Zhang,a   Jun Wu,a   Bin Qiu,*ab   Zhenyu Lin,a   Guonan Chena  and  Zongwei Caib  

* Corresponding authors

a Ministry of Education Key Laboratory of Analysis and Detection for Food Safety, Fujian Provincial Key Laboratory of Analysis and Detection for Food Safety, Fuzhou University, Fuzhou, Fujian 350002, China
E-mail: summer328cn@163.com
Fax: +86-591-22866135

b Department of Chemistry, Hong Kong Baptist University, Hong Kong, China

Abstract

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.

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

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Article information

DOI
https://doi.org/10.1039/C4AY01134A
Article type
Communication
Submitted
12 May 2014
Accepted
14 Jun 2014
First published
16 Jun 2014

Anal. Methods, 2014,6, 8106-8109

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

X. He, H. Zhang, J. Wu, B. Qiu, Z. Lin, G. Chen and Z. Cai, Anal. Methods, 2014, 6, 8106 DOI: 10.1039/C4AY01134A

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