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Bontempi N, Biavardi E, Bordiga D, et al. Probing lysine mono-methylation in histone H3 tail peptides with an abiotic receptor coupled to a non-plasmonic resonator. Nanoscale. 2017;9(25):8639-8646doi: 10.1039/c7nr02491f.
Bontempi, N., Biavardi, E., Bordiga, D., Candiani, G., Alessandri, I., Bergese, P., & Dalcanale, E. (2017). Probing lysine mono-methylation in histone H3 tail peptides with an abiotic receptor coupled to a non-plasmonic resonator. Nanoscale, 9(25), 8639-8646. https://doi.org/10.1039/c7nr02491f
Bontempi, N, et al. "Probing lysine mono-methylation in histone H3 tail peptides with an abiotic receptor coupled to a non-plasmonic resonator." Nanoscale vol. 9,25 (2017): 8639-8646. doi: https://doi.org/10.1039/c7nr02491f
Bontempi N, Biavardi E, Bordiga D, Candiani G, Alessandri I, Bergese P, Dalcanale E. Probing lysine mono-methylation in histone H3 tail peptides with an abiotic receptor coupled to a non-plasmonic resonator. Nanoscale. 2017 Jun 29;9(25):8639-8646. doi: 10.1039/c7nr02491f. PMID: 28608884.
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Nanoscale. 2017 Jun 29;9(25):8639-8646. doi: 10.1039/c7nr02491f.

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

Nanoscale

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

Affiliations

  1. Department of Mechanical and Industrial Engineering, Chemistry for Technologies Laboratory, University of Brescia and INSTM UdR Brescia, Via Branze 38, 25123 Brescia, Italy. [email protected].

PMID: 28608884 DOI: 10.1039/c7nr02491f

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

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