Issue 52, 2016

Supramolecular protection from the enzymatic tyrosine phosphorylation in a polypeptide

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

Supplementary files

Article information

Article type
Communication
Submitted
09 Mud 2016
Accepted
28 Mud 2016
First published
31 Mud 2016
This article is Open Access
Creative Commons BY-NC license

Chem. Commun., 2016,52, 8142-8145

Author version available

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

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