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 journalArticle

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)1-7
Number of pages7
JournalSupramolecular Chemistry
DOIs
StateAccepted/In press - Mar 2 2016

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Enzymes
Lysine
Histone Demethylases
Peptides
Methylation
Gene expression
Histones
Binders
trimethyllysine
tetracyanoresorcin(4)arene
Proteins
p-sulfonatocalix(4)arene

Keywords

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

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Tetracyanoresorcin[4]arene selectively recognises trimethyllysine and inhibits its enzyme-catalysed demethylation. / Peacock, Hayden; Thinnes, Cyrille C.; Kawamura, Akane; Hamilton, Andrew D.

In: Supramolecular Chemistry, 02.03.2016, p. 1-7.

Research output: Contribution to journalArticle

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