Analytical Sciences

Protein-immobilized Electrode for Rapid and Convenient Sensing of Thyroid Hormone Receptor-ligand Interaction

Masaharu MURATA,*  Kentaro YANO,* Shinichiro KUROKI,* Tatsuo SUZUTANI,** and Yoshiki KATAYAMA*

*Department of Applied Chemistry, Graduate School of Engineering, Kyushu University, Fukuoka 812-8581, Japan
**Department of Microbiology, School of Medicine, Fukushima Medical University, 1 Hikarigaoka, Fukushima 960-1295, Japan

The recombinant human thyroid hormone receptor (TR) was expressed as an in-frame fusion with ten consecutive histidine residues using a bacterial system; then the receptor was immobilized on an Au-electrode with Ni(II)-mediated chemisorption using the histidine tag and thiol-modified nitrilotriacetic acid. The receptor-modified electrode could rapidly detect ligand binding to hTR without any separation procedures, and showed a good response in a concentration-dependent manner. The sensitivity of this biosensor based on ligand-receptor interactions was comparable to those of conventional competitive ligand binding assays using radio-labeled ligands. Our results strongly suggest that our new biosensor can be applied to the identification of new ligands for hTR.

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