Jump to main content
Jump to site search
PLANNED MAINTENANCE Close the message box

Scheduled maintenance work on Wednesday 27th March 2019 from 11:00 AM to 1:00 PM (GMT).

During this time our website performance may be temporarily affected. We apologise for any inconvenience this might cause and thank you for your patience.


Issue 52, 2016
Previous Article Next Article

Supramolecular protection from the enzymatic tyrosine phosphorylation in a polypeptide

Author affiliations

Abstract

Here we report two new artificial pseudopeptidic cages that bind the EYE peptide epitope in pure water at physiological pH (as studied by fluorescence and NMR spectroscopies). The supramolecular complexation of the Tyr residues efficiently precludes their subsequent PTK-catalysed phosphorylation. Our results show a supramolecular modulation of the PTK activity by competitive substrate caging.

Graphical abstract: Supramolecular protection from the enzymatic tyrosine phosphorylation in a polypeptide

Back to tab navigation

Supplementary files

Publication details

The article was received on 09 May 2016, accepted on 28 May 2016 and first published on 31 May 2016


Article type: Communication
DOI: 10.1039/C6CC03875A
Author version
available:
Download author version (PDF)
Citation: Chem. Commun., 2016,52, 8142-8145
  • Open access: Creative Commons BY-NC license
  •   Request permissions

    Supramolecular protection from the enzymatic tyrosine phosphorylation in a polypeptide

    E. Faggi, Y. Pérez, S. V. Luis and I. Alfonso, Chem. Commun., 2016, 52, 8142
    DOI: 10.1039/C6CC03875A

    This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material and it is not used for commercial purposes.

    Reproduced material should be attributed as follows:

    • For reproduction of material from NJC:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
    • For reproduction of material from PCCP:
      [Original citation] - Published by the PCCP Owner Societies.
    • For reproduction of material from PPS:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
    • For reproduction of material from all other RSC journals:
      [Original citation] - Published by The Royal Society of Chemistry.

    Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.

Search articles by author

Spotlight

Advertisements