Journal
ANALYTICAL METHODS
Volume 6, Issue 20, Pages 8106-8109Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c4ay01134a
Keywords
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Funding
- NSFC [21375021, 21275031, 21175025]
- Natural Sciences Foundation of Fujian Province [2013J01043]
- Fuzhou Science and Technology Bureau [2012-G-110]
- National Key Technologies R & D Program of China [2012BAD29B06, 2012BAK01B01]
- Major Project of Fujian Province [2011N5008]
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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.
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