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Si us plau utilitzeu sempre aquest identificador per citar o enllaçar aquest document: https://hdl.handle.net/2445/132717
Two-electron connection between tryptophan and phenylalanine/tyrosine residues: linked, constrained and stapled peptides through C-H activation processes
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Natural peptides show high degrees of specificity in their biological action. However, their therapeutical profile is severely limited by their conformational freedom and metabolic instability. Stapled peptides constitute a solution to these problems and access to these structures lies on a limited number of reactions involving the use of non-natural amino acids. Here, we describe a synthetic strategy for the preparation of unique constrained peptides featuring a covalent bond between tryptophan and phenylalanine or tyrosine residues. The preparation of such peptides is achieved in solution and on solid phase directly from the corresponding sequences having an iodo-aryl amino acid through an intramolecular palladium-catalysed C-H activation process. Moreover, complex topologies arise from the internal stapling of cyclopeptides and double intramolecular arylations within a linear peptide. Finally, as a proof of principle, we report the application to this new stapling method to relevant biologically active compounds.
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MENDIVE TAPIA, Lorena, PRECIADO GALLEGO, Sara, GARCÍA, Jesús, RAMÓN, Rosario, KIELLAND, Nicola, ALBERICIO PALOMERA, Fernando, LAVILLA GRÍFOLS, Rodolfo. Two-electron connection between tryptophan and phenylalanine/tyrosine residues: linked, constrained and stapled peptides through C-H activation processes. _Nature Communications_. 2015. Vol. 6, núm. 7160. [consulta: 24 de gener de 2026]. ISSN: 2041-1723. [Disponible a: https://hdl.handle.net/2445/132717]