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    Gold-Nanoparticle-Based Assay for Instantaneous Detection of Nuclear Hormone Receptor−Response Elements Interactions
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    Institute of Material Research and Engineering, ASTAR (Agency for Science, Technology and Research), 3 Research Link, Singapore 117602, and Genome Institute of Singapore, ASTAR (Agency for Science, Technology and Research), 60 Biopolis Street, Singapore 138672
    * Corresponding author. E-mail: [email protected]. Tel: 65-68748420. Fax: 65-68720785.
    †Institute of Material Research and Engineering.
    ‡Genome Institute of Singapore.
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    Analytical Chemistry

    Cite this: Anal. Chem. 2010, 82, 7, 2759–2765
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    https://doi.org/10.1021/ac9026498
    Published March 3, 2010
    Copyright © 2010 American Chemical Society
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    Abstract

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    Gold nanoparticles (AuNPs) are widely used as colorimetric probes for biosensing, relying on their unique particle size-dependent and/or interparticle distance-dependent extinction spectrum and solution color. Herein, we describe an AuNP-based colorimetric assay to detect binding interactions between nuclear hormone receptors and their corresponding DNA-binding elements, particularly the human estrogen receptors (ERα and ERβ) and their cognate estrogen response elements (EREs). We found that the protein−DNA (ER−ERE) complexes can stabilize citrate anion-capped AuNPs against salt-induced aggregation to a larger extent than the protein (ER) or the DNA (ERE) alone, due to their unique molecular size and charge properties that provide a strong electrosteric protection. Moreover, our results show that the extent of stabilization is sequence-dependent and can distinguish a single base variation in the ERE associated with minor changes in protein−DNA binding affinity. With this assay, many important parameters of protein−DNA binding events (e.g., sequence selectivity, distinct DNA binding properties of protein subtypes, binding stoichiometry, and sequence-independent transient binding) can be determined instantly without using labels, tedious sample preparations, and sophisticated instrumentation. These benefits, in particular the high-throughput potential, could enable this assay to become the assay of choice to complement conventional techniques for large scale characterization of protein−DNA interactions, a key aspect in biological research.

    Copyright © 2010 American Chemical Society

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    Supporting Information

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    Negative control results with bovine serum albumin (BSA), amino acids sequence of human ERα, and SPR measurement of the compatibility of ERα−wtERE complex formation and colorimetric detection buffer conditions. This material is available free of charge via the Internet at http://pubs.acs.org.

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    Analytical Chemistry

    Cite this: Anal. Chem. 2010, 82, 7, 2759–2765
    Click to copy citationCitation copied!
    https://doi.org/10.1021/ac9026498
    Published March 3, 2010
    Copyright © 2010 American Chemical Society
    Request reuse permissions

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