Stapling of a 3(10)-helix with click chemistry.

@article{Jacobsen2011StaplingOA,
  title={Stapling of a 3(10)-helix with click chemistry.},
  author={\Oyvind Jacobsen and Hiroaki Maekawa and N H Ge and Carl Henrik G{\"o}rbitz and P{\aa}l Rongved and Ole Petter Ottersen and Mahmood Amiry-Moghaddam and Jo Klaveness},
  journal={The Journal of organic chemistry},
  year={2011},
  volume={76 5},
  pages={1228-38}
}
Short peptides are important as lead compounds and molecular probes in drug discovery and chemical biology, but their well-known drawbacks, such as high conformational flexibility, protease lability, poor bioavailability and short half-lives in vivo, have prevented their potential from being fully realized. Side chain-to-side chain cyclization, e.g., by ring-closing olefin metathesis, known as stapling, is one approach to increase the biological activity of short peptides that has shown promise… CONTINUE READING