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)

文献情報

出版日 2001-05-16

DOI 10.1039/B101807H

インパクトファクター 3.676

著者

Daisuke Hobara, Yusuke Uno, Takashi Kakiuchi

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要旨

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.

掲載誌

Physical Chemistry Chemical Physics

CiteScore: 5.5

自己引用率: 10.3%

年間論文数: 3036

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