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

Hayden Peacock, Cyrille C. Thinnes, Akane Kawamura, Andrew D. Hamilton

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish (US)
Pages (from-to)575-581
Number of pages7
JournalSupramolecular Chemistry
Volume28
Issue number5-6
DOIs
StatePublished - Jun 2 2016

Keywords

  • Host-guest chemistry
  • calixarenes
  • epigenetics
  • histone demethylases
  • resorcinarenes

ASJC Scopus subject areas

  • Chemistry(all)

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