Versatile Matrix for Constructing Enzyme-Based Biosensors

Abstract

A versatile matrix was fabricated and utilized as a universal interface for the construction of enzyme-based biosensors. This matrix was formed on the gold electrode via combining self-assembled monolayer of 2,3-dimercaptosuccinic acid with gold nanoparticles. Gold nanoparticles were electrochemically deposited. Electrochemistry of three redox enzymes (catalase, glucose oxidase, and horseradish peroxidase) was investigated on such a matrix. The electrocatalytic monitoring of hydrogen peroxide and glucose was conducted on this matrix after being coated with those enzymes. On them the monitoring of hydrogen peroxide and glucose shows rapid response times, wide linear working ranges, low detection limits, and high enzymatic affinities. This matrix is thus a versatile and suitable platform to develop highly sensitive enzyme-based biosensors.

Electrocatalytic Properties of Immobilized Heme Proteins: Basic Principles and Applications

“…[1][2][3][4][5] Redox enzymes and modified electron transfer (ET) proteins (in some cases even whole cells or biofilms) immobilized on conductive surfaces were shown to yield efficient and selective bioelectrocatalysis often with better performances than conventional electrodes. Therefore, they are excellent candidates for application in the field of electrocatalysis.…”

“…[1][2][3]26,[29][30][31] The electron transfer pathways through protein monolayers or multilayers (dispersed) films are different and are described by specific models. In this case, information on the ET process can be obtained provided an appropriate experimental design is adopted (e. g. using scan rates high enough to avoid decomposition of the unstable species during the voltammetric measurement).…”

“…[1][2][3][4][5]33,34,38,39] A number of studies obtained the right orientation of ET proteins and redox enzymes using electrode (mainly Au) surfaces functionalized with self-assembled thiol monolayers or with spacers of variable lengths bearing endgroups of different nature. In most cases the term β(r-r 0 ) is large due to the thickness of the polypeptidic shell surrounding the redox center.…”

“…[1][2][3][4][5][6][7][8] Under these conditions, these species can yield efficient and selective bioelectrocatalysis based on direct electron transfer processes. [1][2][3][4][5][6][7][8] Under these conditions, these species can yield efficient and selective bioelectrocatalysis based on direct electron transfer processes.…”

A ‘signal on-off’ electrochemical peptide biosensor for matrix metalloproteinase 2 based on target induced cleavage of a peptide

“…Therefore, it is extremely crucial to 30 develop rapid and sensitive methods for the quantitative detection of MMP-2 in early clinical diagnosis and therapy of tumor. Currently, common methods to detect MMP-2 are mainly involved in immunoassay 7,8 or gelatine zymography 9 , in which the former is expensive and tedious, while the latter is suited for 35 qualitative rather than quantitative analysis. Peptides, short chains of amino acid monomers linked by peptide (amide) bonds, are simple, reliable, cost-effective and resistant to harsh environments [10][11][12] .…”