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E-mail: ywkim730@dongguk.eduReceived April 24, 2013, Accepted June 10, 2013The all-hydrocarbon i,i+4 stapling system using an oct-4-enyl crosslink is one of the most widely employedchemical tools to stabilize an α-helical conformation of a short peptide. This crosslinking system has greatlyextended our ability to modulate intracellular protein-macromolecule interactions. The helix-inducing propertyof the i,i+4 staple has shown to be highly dependent on the length and the stereochemistry of the oct-4-enylcrosslink. Here we show that changing the double bond position within the i,i+4 staple has a considerableimpact not only on the formation of the crosslink but also on α-helix induction. The data further increases theunderstanding of the structure-activity relationships of this valuable chemical tool.Key Words : α-Helix, Stapled peptides, Ring-closing metathesis, Protease resistance, Peptide drugsIntroductionThe α-helix is the most common secondary structurefound in proteins and often plays a critical role in protein-macromolecule interactions in cells.

Comparison of Oct-2-enyl and Oct-4-enyl Staples for Their Formation and α-Helix Stabilizing Effects