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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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Nature Communications, 2015, vol. 6, p. 7160

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cc-by (c) Mendive Tapia, Lorena et al., 2015

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Articles publicats en revistes (Química Inorgànica i Orgànica)

# metadata.dc.title[].value
Two-electron connection between tryptophan and phenylalanine/tyrosine residues: linked, constrained and stapled peptides through C-H activation processes