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Rational Design and Synthesis of Right-Handed D-Sulfono-γ-AApeptide Helical Foldamers as Potent Inhibitors of Protein-Protein Interactions.

Novel unprecedented helical foldamers have been effectively designed and synthesized. The homogeneous right-handed D-sulfono-γ-AApeptides represent a new-generation of unnatural helical peptidomimetics which have similar folding confor-mation to α-peptides, making them an ideal molecular scaffold to design α-helical mimetics. As demonstrated with p53-MDM2 PPI as a model application, the right-handed D-sulfono-γ-AApeptides reveal the much-enhanced binding affinity compared to the p53 peptide. The design of D-sulfono-γ-AApeptides may provide a new and alternative strategy to modulate protein-protein interactions.