[HTML][HTML] Supramolecular protection from the enzymatic tyrosine phosphorylation in a polypeptide
E Faggi, Y Pérez, SV Luis, I Alfonso - Chemical Communications, 2016 - pubs.rsc.org
E Faggi, Y Pérez, SV Luis, I Alfonso
Chemical Communications, 2016•pubs.rsc.orgHere 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.
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.
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.
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