Peptide modification through site-selective residue interconversion: application of the rhodium-catalysed 1,4-addition of aryl siloxanes and boronates

Abstract: The site-selective interconversion of serine and cysteine residues of di- and tripeptides into phenylalanine derivatives, bearing a range of functionalities, has been achieved in high yield and selectivity through the common dehydroalanine intermediate. Through the application and development of the rhodium-catalysed 1,4-addition to α,β-dehydroamino acid moieties with organometallic nucleophiles, a variety of peptides have been successfully modified to contain unnatural amino acid residues in pre-designated residue positions. [Copyright &y& Elsevier]