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

Masaharu Murata, Kentaro Yano, Shinichiro Kuroki, Tatsuo Suzutani, Yoshiki Katayama

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1569-1573
Number of pages5
Journalanalytical sciences
Volume19
Issue number12
DOIs
Publication statusPublished - Dec 2003

Fingerprint

Immobilized Proteins
Thyroid Hormone Receptors
Ligands
Electrodes
Histidine
Biosensors
Nitrilotriacetic Acid
Chemisorption
Sulfhydryl Compounds
Assays
Fusion reactions

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry

Cite this

Protein-immobilized Electrode for Rapid and Convenient Sensing of Thyroid Hormone Receptor-ligand Interaction. / Murata, Masaharu; Yano, Kentaro; Kuroki, Shinichiro; Suzutani, Tatsuo; Katayama, Yoshiki.

In: analytical sciences, Vol. 19, No. 12, 12.2003, p. 1569-1573.

Research output: Contribution to journalArticle

Murata, Masaharu ; Yano, Kentaro ; Kuroki, Shinichiro ; Suzutani, Tatsuo ; Katayama, Yoshiki. / Protein-immobilized Electrode for Rapid and Convenient Sensing of Thyroid Hormone Receptor-ligand Interaction. In: analytical sciences. 2003 ; Vol. 19, No. 12. pp. 1569-1573.
@article{b2f74c6b1b1442a7a74b0051d323cecd,
title = "Protein-immobilized Electrode for Rapid and Convenient Sensing of Thyroid Hormone Receptor-ligand Interaction",
abstract = "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.",
author = "Masaharu Murata and Kentaro Yano and Shinichiro Kuroki and Tatsuo Suzutani and Yoshiki Katayama",
year = "2003",
month = "12",
doi = "10.2116/analsci.19.1569",
language = "English",
volume = "19",
pages = "1569--1573",
journal = "Analytical Sciences",
issn = "0910-6340",
publisher = "The Japan Society for Analytical Chemistry",
number = "12",

}

TY - JOUR

T1 - Protein-immobilized Electrode for Rapid and Convenient Sensing of Thyroid Hormone Receptor-ligand Interaction

AU - Murata, Masaharu

AU - Yano, Kentaro

AU - Kuroki, Shinichiro

AU - Suzutani, Tatsuo

AU - Katayama, Yoshiki

PY - 2003/12

Y1 - 2003/12

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0347915727&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0347915727&partnerID=8YFLogxK

U2 - 10.2116/analsci.19.1569

DO - 10.2116/analsci.19.1569

M3 - Article

C2 - 14696916

AN - SCOPUS:0347915727

VL - 19

SP - 1569

EP - 1573

JO - Analytical Sciences

JF - Analytical Sciences

SN - 0910-6340

IS - 12

ER -