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. Ou...
| Authors: | , , , |
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| Format: | article |
| Status: | Published version |
| Publication Date: | 2016 |
| Country: | España |
| Institution: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repository: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/178169 |
| Online Access: | http://hdl.handle.net/10261/178169 |
| Access Level: | Open access |
| Keyword: | Supramolecular chemistry Bridged Compounds cucurbit[7]uril CB[7 |
| Summary: | 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. © The Royal Society of Chemistry 2016. |
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