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.

Author(s):Nam, E.J., Kim, E.J., Wark, Alastair ORCID: https://orcid.org/0000-0001-8736-7566, Rho, S., Kim, H. and Lee, H.J.
Item type:Article
ID code:37050
Keywords:electrochemical detection , proteins, aptamer-coated gold , nanoparticles, enzyme reactions, Chemistry, Biochemistry, Spectroscopy, Environmental Chemistry, Analytical Chemistry, Electrochemistry
Subjects:Science > Chemistry
Department:Faculty of Science > Pure and Applied Chemistry
Technology and Innovation Centre > Bionanotechnology
Depositing user: Pure Administrator
Date deposited:25 Jan 2012 11:15
Last modified:26 Jul 2019 12:22
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URI:https://strathprints.strath.ac.uk/id/eprint/37050
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