Toggle Main Menu Toggle Search

Open Access padlockePrints

Site-directed introduction of disulfide groups on antibodies for highly sensitive immunosensors

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.

Publication metadata

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


DOI: 10.1007/s00216-016-9630-9


Altmetrics provided by Altmetric