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Tetracyanoresorcin[4]arene selectively recognises trimethyllysine and inhibits its enzyme-catalysed demethylation

Lookup NU author(s): Professor Akane Kawamura

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Abstract

© 2016 Taylor & Francis. Nϵ-methylation of lysine within proteins is a critical biological process that, among other roles, is involved in the control of gene expression. Compounds that recognise Nϵ-methylated lysine may therefore be useful probes for the study of the associated biological mechanisms and have therapeutic potential. Here, we show that tetracyanoresorcin[4]arene (1) selectively recognises Nϵ-trimethyllysine and binds to Nϵ-trimethyllysine within the context of a short peptide. Its binding properties compare favourably to a previously characterised Nϵ-trimethyllysine binder, p-sulfonatocalix[4]arene (2). We also show that both 1 and 2 inhibit the demethylation of Nϵ-trimethyllysine within a histone-derived peptide by the histone demethylase KDM4A.

Publication metadata

Author(s): Peacock H, Thinnes CC, Kawamura A, Hamilton AD

Publication type: Article

Publication status: Published

Journal: Supramolecular Chemistry

Year: 2016

Volume: 28

Issue: 5-6

Pages: 575-581

Online publication date: 07/03/2016

Acceptance date: 06/01/2016

ISSN (print): 1061-0278

ISSN (electronic): 1029-0478

Publisher: Taylor and Francis Ltd

URL: https://doi.org/10.1080/10610278.2016.1140898

DOI: 10.1080/10610278.2016.1140898

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