Supramolecular protection from the enzymatic tyrosine phosphorylation in a polypeptide.
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.
Department of Biological Chemistry and Molecular Modelling, IQAC-CSIC, Jordi Girona 18-26, 08034, Barcelona, Spain. ignacio.alfonso@iqac.csic.es.
Enrico
E
Faggi
NMR Facility, IQAC-CSIC, Jordi Girona 18-26, 08034, Barcelona, Spain.
Yolanda
Y
Pérez
Department of Inorganic and Organic Chemistry, ESTCE Universitat Jaume I, Avd. Sos Baynat, s/n, 12004, Castellón, Spain. luiss@uji.es.
Santiago V
SV
Luis
Department of Biological Chemistry and Molecular Modelling, IQAC-CSIC, Jordi Girona 18-26, 08034, Barcelona, Spain. ignacio.alfonso@iqac.csic.es.
Ignacio
I
Alfonso
D055162:Biocatalysis; D046911:Macromolecular Substances / Q000737:chemistry / Q000378:metabolism; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000737:chemistry / Q000378:metabolism*; D014443:Tyrosine / Q000737:chemistry / Q000378:metabolism*
D046911:Macromolecular Substances; D010455:Peptides; D014443:Tyrosine; D011505:Protein-Tyrosine Kinases