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Lookup NU author(s): Dr Guillaume Suarez, Emeritus Professor Calum McNeilORCiD, Professor Ciara O'Sullivan
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License (CC BY-NC 4.0).
The interface between the sample and the transducer surface is critical to the performance of a biosensor. In this work, we compared different strategies for covalent self-assembly of antibodies onto bare gold substrates by introducing disulfide groups into the immunoglobulin structure, which acted as anchor molecules able to chemisorb spontaneously onto clean gold surfaces. The disulfide moieties were chemically introduced to the antibody via the primary amines, carboxylic acids, and carbohydrates present in its structure. The site-directed modification via the carbohydrate chains exhibited the best performance in terms of analyte response using a model system for the detection of the stroke marker neuron-specific enolase. SPR measurements clearly showed the potential for creating biologically active densely packed self-assembled monolayers (SAMs) in a one-step protocol compared to both mixed SAMs of alkanethiol compounds and commercial immobilization layers. The ability of the carbohydrate strategy to construct an electrochemical immunosensor was investigated using electrochemical impedance spectroscopy (EIS) and differential pulse voltammetry (DPV) transduction.
Author(s): Sanchez JLA, Fragoso A, Joda H, Suarez G, McNeil CJ, O'Sullivan C
Publication type: Article
Publication status: Published
Journal: Analytical and Bioanalytical Chemistry
Year: 2016
Volume: 408
Issue: 19
Pages: 5337-5346
Print publication date: 01/07/2016
Online publication date: 24/05/2016
Acceptance date: 11/05/2016
Date deposited: 17/08/2016
ISSN (print): 1618-2642
ISSN (electronic): 1618-2650
Publisher: Springer
URL: http://dx.doi.org/10.1007/s00216-016-9630-9
DOI: 10.1007/s00216-016-9630-9
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