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Lookup NU author(s): Professor Akane Kawamura
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© 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 tetracyanoresorcinarene (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-sulfonatocalixarene (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.
Author(s): Peacock H, Thinnes CC, Kawamura A, Hamilton AD
Publication type: Article
Publication status: Published
Journal: Supramolecular Chemistry
Online publication date: 07/03/2016
Acceptance date: 06/01/2016
ISSN (print): 1061-0278
ISSN (electronic): 1029-0478
Publisher: Taylor and Francis Ltd
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