Abstract
Polyproline II helix (PPII) is one of the secondary structures in proteins that play an important role in various biological processes. In this study, we have developed a new macrocyclization strategy that efficiently reinforces a model tetrapeptide into a PPII structure. We also elucidated some relationships between structural features and PPII stability in this model. This new macrocyclic stapling strategy can serve as a useful chemical tool to manipulate the PPII structure for various applications.
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