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

Xiaoyan He, Huimin Zhang, Jun Wu, Bin Qiu*, Zhenyu Lin, Guonan Chen, Zongwei CAI

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)8106-8109
Number of pages4
JournalAnalytical Methods
Volume6
Issue number20
DOIs
Publication statusPublished - 21 Oct 2014

Scopus Subject Areas

  • Analytical Chemistry
  • Chemical Engineering(all)
  • Engineering(all)

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