Peptide ligation strategy unlocks diverse range of structural motifs
Approach expected to influence design of protein–protein interaction inhibitors
Researchers in Hong Kong and Germany have unveiled a new chemical ligation strategy to design peptides with a range of complex structural features. The group, led by Xuechen Li at the University of Hong Kong, used benzofuran groups to incorporate salicylaldehyde esters in the peptide side chains, which enabled them to construct a diverse array of peptide scaffolds. The group hopes their work will open new avenues for synthetic peptides and inspire the design of new protein–protein interaction inhibitors, a crucial class of therapeutics for numerous diseases.