Tetracyanoresorcin[4]arene selectively recognises trimethyllysine and inhibits its enzyme-catalysed demethylation. Issue 5 (2nd June 2016)

• Record Type: Journal Article
• Authors: Peacock, Hayden; Thinnes, Cyrille C.; Kawamura, Akane; Hamilton, Andrew D.
• Is Part Of: Supramolecular chemistry. Volume 28:Issue 5/6(2016)
• Page Start: 575
• Page End: 581
• Publication Date: 2016-06-02
• Subjects: Host-guest chemistry -- resorcinarenes -- calixarenes -- histone demethylases -- epigenetics; Macromolecules -- Periodicals; Supramolecular chemistry -- Periodicals; 547.005
• DOI: 10.1080/10610278.2016.1140898
• Languages: English
• ISSNs: 1061-0278

Abstract

Abstract: N ε-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 N ε-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 N ε-trimethyllysine and binds to N ε-trimethyllysine within the context of a short peptide. Its binding properties compare favourably to a previously characterised N ε-trimethyllysine binder, p -sulfonatocalix[4]arene ( 2 ). We also show that both 1 and 2 inhibit the demethylation of N ε-trimethyllysine within a histone-derived peptide by the histone demethylase KDM4A. Abstract :