A facile synthetic strategy for constructing diverse peptide structural architectures via chemoselective peptide ligation was developed. The key advancement involved is to utilize the benzofuran moiety as the peptide salicylaldehyde ester surrogate, and hydroxyl lysine building block or Dap-Ser / Lys-Ser dipeptide as the hydroxyl amino functionality. In addition to the side chain-to-side chain cyclic peptides, three classes of structural motifs have been designed and successfully synthesized with native peptidic linkages at the ligation sites, including Class I: branched and bridged peptides, Class II: tailed cyclic peptides and Class III: bridged cyclic peptides and bicyclic peptides. These results have demonstrated the flexibility of the chemical ligation approach to construct diverse peptide structural architectures. We anticipate that this strategy will provide an alternative strategic opportunity for synthetic peptide development. It also serves as an inspiration for the structural design of protein-protein interactions (PPIs) inhibitors with new modalities.

Construction of Diverse Peptide Structural Architectures via Chemoselective Peptide Ligation

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