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Fast Screening of Ligand-Protein Interactions based on Ligand-Induced Protein Stabilization of Gold Nanoparticles

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Download Hi-Res ImageDownload to MS-PowerPointCite This:Anal. Chem. 2014, 86, 5, 2361-2370
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    Fast Screening of Ligand-Protein Interactions based on Ligand-Induced Protein Stabilization of Gold Nanoparticles
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    † Institute of Materials Research and Engineering, Agency for Science, Technology and Research (A*STAR), 3 Research Link, 117602 Singapore
    ‡ Cancer Biology and Pharmacology, Genome Institute of Singapore, Agency for Science, Technology and Research (A*STAR), 60 Biopolis Street, 138672 Singapore
    § Department of Chemistry, University of Illinois at Urbana−Champaign, Urbana, Illinois 61801, United States
    *E-mail: [email protected]
    *E-mail: [email protected]
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    Analytical Chemistry

    Cite this: Anal. Chem. 2014, 86, 5, 2361–2370
    Click to copy citationCitation copied!
    https://doi.org/10.1021/ac404241y
    Published January 31, 2014
    Copyright © 2014 American Chemical Society
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    Abstract

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    High throughput screening of small molecular weight (LMW) ligands for protein and sensitive determination of ligand-induced protein stabilization is an important task in drug discovery and in protein structural and functional genomics studies. In this study, gold nanoparticles (AuNPs) and their aggregation property are used to develop a rapid and less equipment intensive assay for screening the interactions between LMW ligands and transcription factors (TFs) and human serum albumin. The assay is based on the fact that the aggregation/discpersion status of AuNPs is very sensitive to the conformation of surrounding proteins, and when a LMW ligand binds to the proteins, it can enhance proteins’ salt and thermal stability, and therefore the protective effect on AuNPs from aggregation. Two TFs, i.e. FoxA1 (Forkhead box A1) and AP-2γ (activating enhancer binding protein 2 gamma), and 14 compounds from an NCI compounds library and human serum albumin (HSA) and three known ligands (ibuprofen, warfarin, and phenytoin) are involved to demonstrate the concept and to prove its generality and robustness. With this AuNP method, two strong LMW binders are identified for FoxA1 and AP-2γ; ligand induced protein stabilization is determined. The results have been verified using surface plasmon resonance spectroscopy (SPR) and differential static light scattering (DSLS) techniques. Tryptophan fluorescent measurement is also conducted to provide further information on protein conformational change upon LMW ligand loading as can be observed from AuNPs’ UV–vis spectra. FoxA1 and AP-2γ are pivotal in regulating the transcriptional activity of estrogen receptor alpha and controlling the expression of estrogen-responsive breast cancer cells. Identification of drug candidates targeting these two transcription factors could be an alternative in treating breast cancer, in particular those that have become endocrine resistance.

    Copyright © 2014 American Chemical Society

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    Analytical Chemistry

    Cite this: Anal. Chem. 2014, 86, 5, 2361–2370
    Click to copy citationCitation copied!
    https://doi.org/10.1021/ac404241y
    Published January 31, 2014
    Copyright © 2014 American Chemical Society
    Request reuse permissions

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