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World class computing and information science research at Strathclyde...

The Strathprints institutional repository is a digital archive of University of Strathclyde's Open Access research outputs. Strathprints provides access to thousands of Open Access research papers by University of Strathclyde researchers, including by researchers from the Department of Computer & Information Sciences involved in mathematically structured programming, similarity and metric search, computer security, software systems, combinatronics and digital health.

The Department also includes the iSchool Research Group, which performs leading research into socio-technical phenomena and topics such as information retrieval and information seeking behaviour.

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Highly-sensitive electrochemical detection of proteins using aptamer-coated gold nanoparticles and surface enzyme reactions

Nam, E.J. and Kim, E.J. and Wark, Alastair and Rho, S. and Kim, H. and Lee, H.J. (2012) Highly-sensitive electrochemical detection of proteins using aptamer-coated gold nanoparticles and surface enzyme reactions. Analyst, 137. pp. 2011-2016. ISSN 0003-2654

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Abstract

Gold nanoparticle (NP) enhanced surface sandwich assays for the detection of proteins is developed in conjunction with a surface enzyme reaction. As a model protein, immunoglobulin E (IgE) possessing two different epitopes for anti-IgE and IgE specific aptamer is used. A surface sandwich was first formed via the adsorption of IgE onto IgE aptamer coated Au NP-modified gold electrodes followed by the specific interaction of alkaline phosphatase (ALP) conjugated anti-IgE onto the surface IgE complex. The selective electrochemical signal was then achieved by measuring released electrons from the reaction of the substrate, 4-aminophenylphosphate (APP) with the surface IgE-aptamer-NPs/IgE/anti-IgE-ALP complex. The signal enhancement effect of NPs in ALP amplified assays was also studied using the IgE aptamer/IgE/antiIgE-ALP complex. The use of aptamer coated NPs with the enzymatically amplified sandwich assay resulted in an excellent enhancement for IgE detection and a significant reduction of non-specific adsorption events.