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Probing lysine mono-methylation in histone H3 tail peptides with an abiotic receptor coupled to a non-plasmonic resonator

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Abstract

Binder and effector molecules that allow studying and manipulating epigenetic processes are of biological relevance and pose severe technical challenges. We report the first example of a synthetic receptor able to recognize mono-methylated lysines in a histone H3 tail peptide, which has relevant functions in epigenetic regulation. Recognition is robust and specific regardless of the position and the number of mono-methylated lysines along the polypeptide chain. The peptide is first captured in solution by a tetraphosphonate cavitand (Tiiii) that selectively binds its Lys-NMe+ moieties. Separation from solution and detection of the peptide-Tiiii complexes is then enabled in one single step by an all dielectric SiO2–TiO2 core–shell resonator (T-rex), which captures the complex and operates fully reproducible signal transduction by non-plasmonic surface enhanced Raman scattering (SERS) without degrading the complex. The realized abiotic probe is able to distinguish multiple mono-methylated peptides from the single mono-methylated ones.

Graphical abstract: Probing lysine mono-methylation in histone H3 tail peptides with an abiotic receptor coupled to a non-plasmonic resonator

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Publication details

The article was received on 07 Apr 2017, accepted on 18 May 2017 and first published on 19 May 2017


Article type: Paper
DOI: 10.1039/C7NR02491F
Citation: Nanoscale, 2017, Advance Article
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    Probing lysine mono-methylation in histone H3 tail peptides with an abiotic receptor coupled to a non-plasmonic resonator

    N. Bontempi, E. Biavardi, D. Bordiga, G. Candiani, I. Alessandri, P. Bergese and E. Dalcanale, Nanoscale, 2017, Advance Article , DOI: 10.1039/C7NR02491F

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