A new i, i + 3 peptide stapling system for α-helix stabilization

We have previously shown that the incorporation of an 8-atom all-hydrocarbon 'staple' at positions i and i + 3 of a synthetic peptide results in substantial stabilization of the α-helical conformation. As part of our ongoing effort to explore the scope and utility of all-hydrocarbon stapling systems, we have investigated and report herein the properties of a new i, i + 3 stapling system that employs a 6-carbon cross-link. As part of our ongoing effort to explore the scope and utility of all-hydrocarbon peptide stapling systems, we have investigated and report herein the properties of a new i, i + 3 stapling system that employs a 6-carbon cross-link.