Immobilization of azurin with retention of its native electrochemical properties at alkylsilane self-assembled monolayer modified indium tin oxide

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Indium tin oxide (ITO) is a promising material for developing spectroelectrochemical methods due to its combination of excellent transparency in the visible region and high conductivity over a broad range of potential. However, relatively few examples of immobilization of redox proteins at ITO with retention of the ability to transfer electrons with the underlying material with native characteristics have been reported. In this work, we utilize an alkylsilane functionalized ITO surface as a biocompatible interface for immobilization of the blue copper protein azurin. Adsorption of azurin at ITO as well as ITO coated with self-assembled monolayers of (3-mercaptopropyl) trimethoxysilane (MPTMS) and n-decyltrimethoxysilane (DTMS) was achieved, and immobilized protein probed using protein film electrochemistry. The native redox properties of the protein were perturbed by adsorption directly to ITO or to the MPTMS layer on an ITO surface. However, azurin adsorbed at a DTMS covered ITO surface retained native electrochemical properties (E1/2 = 122 ± 5 mV vs. Ag/AgCl) and could exchange electrons directly with the underlying ITO layer without need for an intervening chemical mediator. These results open new opportunities for immobilizing functional redox proteins at ITO and developing spectroelectrochemical methods for investigating them.

Original languageEnglish
Pages (from-to)169-174
Number of pages6
JournalElectrochimica Acta
Volume85
DOIs
Publication statusPublished - Dec 15 2012

Fingerprint

Azurin
Self assembled monolayers
Tin oxides
Electrochemical properties
Indium
Proteins
indium tin oxide
Immobilized Proteins
Adsorption
Electrons
Electrochemistry
Transparency
Copper

Keywords

  • Azurin
  • Immobilized redox proteins
  • Indium tin oxide
  • Monolayer
  • Protein film electrochemistry

ASJC Scopus subject areas

  • Electrochemistry
  • Chemical Engineering(all)

Cite this

@article{853382b95bcc44ac82998e59f1fd74a6,
title = "Immobilization of azurin with retention of its native electrochemical properties at alkylsilane self-assembled monolayer modified indium tin oxide",
abstract = "Indium tin oxide (ITO) is a promising material for developing spectroelectrochemical methods due to its combination of excellent transparency in the visible region and high conductivity over a broad range of potential. However, relatively few examples of immobilization of redox proteins at ITO with retention of the ability to transfer electrons with the underlying material with native characteristics have been reported. In this work, we utilize an alkylsilane functionalized ITO surface as a biocompatible interface for immobilization of the blue copper protein azurin. Adsorption of azurin at ITO as well as ITO coated with self-assembled monolayers of (3-mercaptopropyl) trimethoxysilane (MPTMS) and n-decyltrimethoxysilane (DTMS) was achieved, and immobilized protein probed using protein film electrochemistry. The native redox properties of the protein were perturbed by adsorption directly to ITO or to the MPTMS layer on an ITO surface. However, azurin adsorbed at a DTMS covered ITO surface retained native electrochemical properties (E1/2 = 122 ± 5 mV vs. Ag/AgCl) and could exchange electrons directly with the underlying ITO layer without need for an intervening chemical mediator. These results open new opportunities for immobilizing functional redox proteins at ITO and developing spectroelectrochemical methods for investigating them.",
keywords = "Azurin, Immobilized redox proteins, Indium tin oxide, Monolayer, Protein film electrochemistry",
author = "Idan Ashur and Jones, {Anne Katherine}",
year = "2012",
month = "12",
day = "15",
doi = "10.1016/j.electacta.2012.08.044",
language = "English",
volume = "85",
pages = "169--174",
journal = "Electrochimica Acta",
issn = "0013-4686",
publisher = "Elsevier Limited",

}

TY - JOUR

T1 - Immobilization of azurin with retention of its native electrochemical properties at alkylsilane self-assembled monolayer modified indium tin oxide

AU - Ashur, Idan

AU - Jones, Anne Katherine

PY - 2012/12/15

Y1 - 2012/12/15

N2 - Indium tin oxide (ITO) is a promising material for developing spectroelectrochemical methods due to its combination of excellent transparency in the visible region and high conductivity over a broad range of potential. However, relatively few examples of immobilization of redox proteins at ITO with retention of the ability to transfer electrons with the underlying material with native characteristics have been reported. In this work, we utilize an alkylsilane functionalized ITO surface as a biocompatible interface for immobilization of the blue copper protein azurin. Adsorption of azurin at ITO as well as ITO coated with self-assembled monolayers of (3-mercaptopropyl) trimethoxysilane (MPTMS) and n-decyltrimethoxysilane (DTMS) was achieved, and immobilized protein probed using protein film electrochemistry. The native redox properties of the protein were perturbed by adsorption directly to ITO or to the MPTMS layer on an ITO surface. However, azurin adsorbed at a DTMS covered ITO surface retained native electrochemical properties (E1/2 = 122 ± 5 mV vs. Ag/AgCl) and could exchange electrons directly with the underlying ITO layer without need for an intervening chemical mediator. These results open new opportunities for immobilizing functional redox proteins at ITO and developing spectroelectrochemical methods for investigating them.

AB - Indium tin oxide (ITO) is a promising material for developing spectroelectrochemical methods due to its combination of excellent transparency in the visible region and high conductivity over a broad range of potential. However, relatively few examples of immobilization of redox proteins at ITO with retention of the ability to transfer electrons with the underlying material with native characteristics have been reported. In this work, we utilize an alkylsilane functionalized ITO surface as a biocompatible interface for immobilization of the blue copper protein azurin. Adsorption of azurin at ITO as well as ITO coated with self-assembled monolayers of (3-mercaptopropyl) trimethoxysilane (MPTMS) and n-decyltrimethoxysilane (DTMS) was achieved, and immobilized protein probed using protein film electrochemistry. The native redox properties of the protein were perturbed by adsorption directly to ITO or to the MPTMS layer on an ITO surface. However, azurin adsorbed at a DTMS covered ITO surface retained native electrochemical properties (E1/2 = 122 ± 5 mV vs. Ag/AgCl) and could exchange electrons directly with the underlying ITO layer without need for an intervening chemical mediator. These results open new opportunities for immobilizing functional redox proteins at ITO and developing spectroelectrochemical methods for investigating them.

KW - Azurin

KW - Immobilized redox proteins

KW - Indium tin oxide

KW - Monolayer

KW - Protein film electrochemistry

UR - http://www.scopus.com/inward/record.url?scp=84866870432&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84866870432&partnerID=8YFLogxK

U2 - 10.1016/j.electacta.2012.08.044

DO - 10.1016/j.electacta.2012.08.044

M3 - Article

AN - SCOPUS:84866870432

VL - 85

SP - 169

EP - 174

JO - Electrochimica Acta

JF - Electrochimica Acta

SN - 0013-4686

ER -