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Design of an Automated Electrochemical Biosensor Modified with Phenylboronic Acid to Study Glycoprotein Immobilization
Author(s) -
Ölçer Zehra
Publication year - 2020
Publication title -
chemistryselect
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.437
H-Index - 34
ISSN - 2365-6549
DOI - 10.1002/slct.202002628
Subject(s) - phenylboronic acid , boronic acid , biosensor , horseradish peroxidase , chemistry , glutaraldehyde , amperometry , glycoprotein , self assembled monolayer , covalent bond , layer (electronics) , combinatorial chemistry , electrode , electrochemistry , chromatography , nanotechnology , monolayer , biochemistry , organic chemistry , materials science , enzyme , catalysis
It is important that biosensor surface chemistry assays because of the easy immobilization of biological sensing molecules on the chip surface and especially not damage of these molecules through surface effects. Boronic acid modified self‐assembled monolayers can be formed on gold electrodes and used immobilizations of glycoproteins. Glycoproteins which have short oligosaccharides exist in various cellular events with different functions and serve in many cellular events as cell surface recognition. It was successfully fabricated a new phenylboronic acid self‐assembled layer on gold electrodes for immobilization of glycoproteins, where 4‐aminophenylboronic acid (APBA) is covalently bound to the 11‐mercapto‐1‐undecanol (MUOL) layer with glutaraldehyde linkage. The specific binding of glycoprotein with self‐assebled layer was studied using horseradish peroxidase (HRP) as a model protein. All the experiments, voltametric and amperometric measurements were carried out during microfluidic flow first time using automated new biosensor device that enabled fast and easy modification of electrode surface with boronic acid and immobilization of the HRP protein in a short period of time.