Document Type

Journal Article

Department/Unit

Department of Chemistry

Title

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

Language

English

Abstract

© the Partner Organisations 2014. 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.

Publication Date

2014

Source Publication Title

Analytical Methods

Volume

6

Issue

20

Start Page

8106

End Page

8109

Publisher

Royal Society of Chemistry

DOI

10.1039/c4ay01134a

Link to Publisher's Edition

http://dx.doi.org/10.1039/c4ay01134a

ISSN (print)

17599660

ISSN (electronic)

17599679

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