Goode, J orcid.org/0000-0002-3642-1291, Dillon, G and Millner, PA orcid.org/0000-0002-4813-4302 (2016) The development and optimisation of Nanobody based electrochemical immunosensors for IgG. Sensors and Actuators B: Chemical, 234. pp. 478-484. ISSN 0925-4005
Abstract
Biosensors are increasingly heralded for their potential to create inexpensive diagnostic devices which are sensitive, selective and easy to use. One of the key categories of biosensor are immunosensors, which have historically used antibodies as bioreceptors. Though widely used, antibodies bring inherent limitations such as variability, limited stability and their reliance on animal sources. This has led to the development of alternative immuno-reagents such as non-antibody binding proteins (NABPs). These are low molecular weight proteins which largely avoid the aforementioned advantages of antibodies. They are commonly produced by bacteria enabling the use of DNA technology to manipulate bioreceptors at the molecular level. Single chain VHHs (commonly known as nanobodies) are an antibody derived NABP adapted from camelid heavy chain antibodies which are the isolated binding domain. Whilst nanobodies have been used for diagnostic and therapeutic applications, they have limited demonstration in biosensors. In this study, both antibodies and nanobodies were used to construct a biosensor. In addition nanobody performance was optimised by introducing a novel peptide spacer. The role of nanobody orientation and spacing was thus investigated and spacer length was optimised, leading to an increase in the sensitivity of the biosensor.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2016 Elsevier B.V. All rights reserved. This is an author produced version of a paper published in Sensors and Actuators B: Chemical. Uploaded in accordance with the publisher's self-archiving policy. |
Keywords: | Nanobody; Impedance; Immunosensor; Orientation; Spacer; Steric Hindrance |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Biomedical Sciences (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 13 May 2016 10:07 |
Last Modified: | 05 Apr 2018 07:14 |
Published Version: | http://dx.doi.org/10.1016/j.snb.2016.04.132 |
Status: | Published |
Publisher: | Elsevier |
Identification Number: | 10.1016/j.snb.2016.04.132 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:99492 |