2026-04-13T02:28:02Zhttps://recercat.cat/oai/request
oai:recercat.cat:2445/1327172025-12-04T21:44:01Zcom_2072_1057col_2072_478917col_2072_478933
RECERCAT author Mendive Tapia, Lorena author Preciado Gallego, Sara author García, Jesús author Ramón, Rosario author Kielland, Nicola author Albericio Palomera, Fernando author Lavilla Grífols, Rodolfo 2019-05-06T09:46:47Z2019-05-06T09:46:47Z2015-05-212019-05-06T09:46:48Z 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. cc-by (c) Mendive Tapia, Lorena et al., 2015 http://creativecommons.org/licenses/by/3.0/es info:eu-repo/semantics/openAccess Síntesi en fase sólida Química combinatòria Ressonància magnètica nuclear Solid-phase synthesis Combinatorial chemistry Nuclear magnetic resonance Two-electron connection between tryptophan and phenylalanine/tyrosine residues: linked, constrained and stapled peptides through C-H activation processes info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion