@article{oai:nagasaki-u.repo.nii.ac.jp:00026819,
 author = {Makura, Yui and Ueda, Atsushi and Kato, Takuma and Iyoshi, Akihiro and Higuchi, Mei and Doi, Mitsunobu and Tanaka, Masakazu},
 issue = {10},
 journal = {International Journal of Molecular Sciences},
 month = {May},
 note = {Hydrocarbon stapling is a useful tool for stabilizing the secondary structure of peptides. Among several methods, hydrocarbon stapling at i,i + 1 positions was not extensively studied,  and their secondary structures are not clarified. In this study, we investigate i,i + 1 hydrocarbon stapling between cis-4-allyloxy-L-proline and various olefin-tethered amino acids. Depending on the ring size of the stapled side chains and structure of the olefin-tethered amino acids, E- or Z-selectivities were observed during the ring-closing metathesis reaction (E/Z was up to 8.5:1 for 17–14-membered rings and up to 1:20 for 13-membered rings). We performed X-ray crystallographic analysis of hydrocarbon stapled peptide at i,i + 1 positions. The X-ray crystallographic structure suggested that the i,i + 1 staple stabilizes the peptide secondary structure to the right-handed α-helix. These findings are especially important for short oligopeptides because the employed stapling method uses two minimal amino acid residues adjacent to each other., International Journal of Molecular Sciences, 22(10), art. no. 5364; 2021},
 title = {X-ray crystallographic structure of α-helical peptide stabilized by hydrocarbon stapling at i,i + 1 positions},
 volume = {22},
 year = {2021}
}