Abstract
A photoredox-catalyzed oxidative decarboxylative coupling of small peptides is reported, giving access to a variety of N,O-acetals. They were used as intermediates for the addition of phenols and indoles, leading to novel peptide scaffolds and bioconjugates. Amino acids with nucleophilic side chains, such as serine, threonine, tyrosine and tryptophan, could also be used as partners to access tri- and tetrapeptide derivatives with non-natural cross-linking.
Highlights
Bioactive peptides have gained a lot of attention in the past decade as therapeutic compounds interacting with receptors or inhibiting protein–protein interactions
The biological activity and metabolic stability of native peptides is usually improved by the introduction of unnatural amino-acids (UAA) and rigidifying elements.[1]
The scope of nucleophiles included alcohols and electron-rich aromatic residues present in natural amino acids such as serine, threonine, tyrosine and tryptophan, giving access to new types of peptide cross-linking for the synthesis of non-natural tri- and tetrapeptides
Summary
Bioactive peptides have gained a lot of attention in the past decade as therapeutic compounds interacting with receptors or inhibiting protein–protein interactions. The advent of photoredox catalysis contributed to the development of new strategies for bioconjugation via one– electron processes (Scheme 1A).[13] Starting from native peptides, C-terminal decarboxylative arylation,[14] reduction,[15] allylation,[16] alkynylation,[17] cyanation,[18] azidation[19] and Giese coupling[20] have been described. The scope of nucleophiles included alcohols and electron-rich aromatic residues present in natural amino acids such as serine, threonine, tyrosine and tryptophan, giving access to new types of peptide cross-linking for the synthesis of non-natural tri- and tetrapeptides
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