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

Year: 2017

Authors: Bontempi N., Biavardi E., Bordiga D., Candiani G., Alessandri I., Bergese P., Dalcanale E.

Autors Affiliation: Department of Mechanical and Industrial Engineering, Chemistry for Technologies Laboratory, University of Brescia, INSTM UdR Brescia, Via Branze 38, Brescia, 25123, Italy; Department of Chemistry, Life Science and Environmental Sustainability, University of Parma, INSTM UdR Parma, Parco Area delle Scienze 17/A, Parma, 43124, Italy; Department of Molecular and Translational Medicine, University of Brescia, INSTM UdR Brescia, Viale Europa 11, Brescia, 25123, Italy; Department of Chemistry, Materials and Chemical Engineering G. Natta, Polytechnic of Milan, INSTM UdR Milano, Via Mancinelli 7, Milano, 20131, Italy

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.

Journal/Review: NANOSCALE

Volume: 9 (25)      Pages from: 8639  to: 8646

More Information: This work was supported by SUPRANANO (INSTM-Regione Lombardia project). Centro Intefacolta di Misure \”G. Casnati\” of the University of Parma is acknowledged for the use of NMR facilities. We thank Matteo Ferroni for support in SEM analysis.
KeyWords: e da rivista: Alkylation; Amino acids; Bins; Clouds; Peptides; Plasmons; Raman scattering; Resonators; Signal transduction; Surface scattering, Core shell; Epigenetic regulation; Plasmonic resonators; Polypeptide chain; Single-step; Surface enhanced Raman Scattering (SERS); Synthetic receptors; Technical challenges, Proteins
DOI: 10.1039/c7nr02491f

Citations: 22
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