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

doi:10.1039/c4ay01134a

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

Department of Chemistry

Research output: Contribution to journal › Journal article › peer-review

3 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 language	English
Pages (from-to)	8106-8109
Number of pages	4
Journal	Analytical Methods
Volume	6
Issue number	20
DOIs	https://doi.org/10.1039/c4ay01134a
Publication status	Published - 21 Oct 2014

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

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.",

author = "Xiaoyan He and Huimin Zhang and Jun Wu and Bin Qiu and Zhenyu Lin and Guonan Chen and Zongwei CAI",

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T1 - Fluorescence probe techniques to study the interaction between hydroxylated polybrominated diphenyl ethers (OH-PBDEs) and protein disulfide isomerase (PDI)

AU - He, Xiaoyan

AU - Zhang, Huimin

AU - Wu, Jun

AU - Qiu, Bin

AU - Lin, Zhenyu

AU - Chen, Guonan

AU - CAI, Zongwei

PY - 2014/10/21

Y1 - 2014/10/21

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/84907482625

U2 - 10.1039/c4ay01134a

DO - 10.1039/c4ay01134a

M3 - Journal article

AN - SCOPUS:84907482625

SN - 1759-9660

VL - 6

SP - 8106

EP - 8109

JO - Analytical Methods

JF - Analytical Methods

IS - 20

ER -

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

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