Issue 16, 2001

Immobilization of horseradish peroxidase on nanometre-scale domains of binary self-assembled monolayers formed from dithiobis-N-succinimidyl propionate and 1-tetradecanethiol on Au(111)

Abstract

The nanometre-scale, domain-specific immobilization of horseradish peroxidase (HRP) on binary self-assembled monolayers (SAMs) of dithiobis-N-succinimidyl propionate (DTSP) and 1-tetradecanethiol (TDT) formed on Au(111) has been confirmed by X-ray photoelectron spectroscopy (XPS) and atomic force microscopy. After immersing the Au substrates modified with the binary SAMs into an HRP solution, XPS spectra show significant increases in the peak areas of N(1s) and O(1s), indicating the presence of HRP on the surface. After rinsing of the substrate with a KCl solution only covalently immobilized HRP molecules on the domains composed of DTSP remain on the surface. The enzymatic activity of the immobilized HRP is confirmed using cyclic voltammetry in the presence of catechol as an electron transfer mediator.

Article information

Article type
Paper
Submitted
26 Feb 2001
Accepted
06 Apr 2001
First published
16 May 2001

Phys. Chem. Chem. Phys., 2001,3, 3437-3441

Immobilization of horseradish peroxidase on nanometre-scale domains of binary self-assembled monolayers formed from dithiobis-N-succinimidyl propionate and 1-tetradecanethiol on Au(111)

D. Hobara, Y. Uno and T. Kakiuchi, Phys. Chem. Chem. Phys., 2001, 3, 3437 DOI: 10.1039/B101807H

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