Recognition of proximally phosphorylated tyrosine residues and continuous analysis of phosphatase activity using a stable europium complex
journal contributionposted on 2018-02-01, 12:13 authored by Sarah Hewitt, Roanna Liu, Stephen ButlerStephen Butler
The recognition of proteins and their post-translational modifications using synthetic molecules is an active area of research. A common post-translational modification is the phosphorylation of serine, threonine or tyrosine residues. The phosphorylation of proximal tyrosine residues occurs in over 1000 proteins in the human proteome, including in disease-related proteins, so the recognition of this motif is of particular interest. We have developed a luminescent europium(III) complex, [Eu.1] + , capable of the discrimination of proximally phosphorylated tyrosine residues, from analogous mono- and non-phosphorylated tyrosine residues, more distantly-related phosphotyrosine residues and over proximally phosphorylated serine and threonine residues. [Eu.1] + was used to continuously monitor the phosphatase catalysed dephosphorylation of a peptide containing proximally phosphorylated tyrosine residues.
This work was supported by a Wellcome Trust Seed Award [grant number 204500/Z/16/Z] and The Royal Society [Research Grant (RG150476)].
Published inSupramolecular Chemistry
Pages765 - 771
CitationHEWITT, S.H., LIU, R. and BUTLER, S.J., 2017. Recognition of proximally phosphorylated tyrosine residues and continuous analysis of phosphatase activity using a stable europium complex. Supramolecular Chemistry, 30 (9), pp. 765-771.
Publisher© Taylor and Francis
- AM (Accepted Manuscript)
Publisher statementThis work is made available according to the conditions of the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0) licence. Full details of this licence are available at: https://creativecommons.org/licenses/by-nc-nd/4.0/
NotesThis is an Accepted Manuscript of an article published by Taylor & Francis in Supramolecular Chemistry on 30 November 2017, available online: http://www.tandfonline.com/10.1080/10610278.2017.1410548.