Variable-Length Ester-Based Staples for α-Helical Peptides by Using A Double Thiol-ene Reaction.

摘要: A novel peptide stapling method effected by a double thiol-ene reaction between two cysteine residues and divinyl diester to access stapled peptides with enhanced cell permeability is reported. This diverse chemical tool kit provides facile varying bridge lengths. Stapled Axin mimetics were synthesised using this resulting in improved α-helicity relative the unstapled peptide. Cell penetrating analogues of SIGK that targets protein-protein interaction hotspot Gβγ proteins also exhibited moderate increase permeable. chemoselective highly amenable as easily modify synthetic α-helical target intracellular proteins.