New peptide architectures through C–H activation stapling between tryptophan–phenylalanine/tyrosine residues

Lorena Mendive-Tapia, Sara Preciado, Jesús García, Rosario Ramón, Nicola Kielland, Fernando Albericio () and Rodolfo Lavilla ()
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Lorena Mendive-Tapia: Institute for Research in Biomedicine, Barcelona Science Park
Sara Preciado: University of Barcelona
Jesús García: Institute for Research in Biomedicine, Barcelona Science Park
Rosario Ramón: Barcelona Science Park
Nicola Kielland: Barcelona Science Park
Fernando Albericio: Institute for Research in Biomedicine, Barcelona Science Park
Rodolfo Lavilla: Barcelona Science Park

Nature Communications, 2015, vol. 6, issue 1, 1-9

Abstract: Abstract 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.

Date: 2015
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DOI: 10.1038/ncomms8160

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