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Issue 21, 2018
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High-affinity binding with specific peptides endows EuW10 a good luminescence probe for HPV E6 detection

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Abstract

Human papillomavirus (HPV) E6, acting as a major oncoprotein of high-risk sub-type, is known as an ideal biomarker with diagnostic potential. Due to the bottleneck lacking effective, commercially available mono-clonal antibody (mAbs) for HPV16 E6, we report a new luminescence protocol for the in vitro E6 detection in the present study. By selecting an inorganic cluster, Na9[EuW10O36]·32H2O (EuW10) that contains nine negative charges as a fluorescence probe, a concentration as low as 0.28 μM for HPV16 E6 was detectable in buffer solution. For that, a small peptide rich in basic residues from E6 was used to construct the platform for the high-affinity interaction assay of protein to EuW10. Additionally, the binding mechanism between EuW10 with peptide and protein was revealed in detail by time-resolved fluorescence spectrometry and ITC, while the binding processes were monitored by TEM images. Therefore, the present study not only provides a practical support for the application of polyoxometalate (POM) clusters as biological probes to HPV E6 detection, but also is significant for the early diagnosis of HPV-induced cancers.

Graphical abstract: High-affinity binding with specific peptides endows EuW10 a good luminescence probe for HPV E6 detection

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Publication details

The article was received on 07 Aug 2018, accepted on 19 Sep 2018 and first published on 22 Sep 2018


Article type: Paper
DOI: 10.1039/C8NJ03981J
Citation: New J. Chem., 2018,42, 17339-17345

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    High-affinity binding with specific peptides endows EuW10 a good luminescence probe for HPV E6 detection

    Y. Liu, X. Yuan, W. Wang, Y. Wu and L. Wu, New J. Chem., 2018, 42, 17339
    DOI: 10.1039/C8NJ03981J

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