Multicyclic peptides have the potential to mimic the antigen-binding potency of the complementarity-determining regions of antibodies, enabling the development of potent peptide binders to challenging targets, but the scaffolds of multicyclic peptides are difficult to engineer. Here, the authors design a range of triscysteine motifs with disulfide-directing capability for regulating the oxidative folding of multicyclic peptides and employ them in the design of disulfide-directed multicyclic peptide libraries for discovery of potent peptide binders.
- Zengping Duan
- Chuilian Kong
- Chuanliu Wu
