التفاصيل البيبلوغرافية
| العنوان: |
X-ray Crystallographic Structure of α-Helical Peptide Stabilized by Hydrocarbon Stapling at i , i + 1 Positions. |
| المؤلفون: |
Makura, Yui, Ueda, Atsushi, Kato, Takuma, Iyoshi, Akihiro, Higuchi, Mei, Doi, Mitsunobu, Tanaka, Masakazu, Ruvo, Menotti, Doti, Nunzianna |
| المصدر: |
International Journal of Molecular Sciences; May2021, Vol. 22 Issue 10, p5364-5364, 1p |
| مصطلحات موضوعية: |
HYDROCARBON analysis, X-rays, HYDROCARBONS, METATHESIS reactions, OLIGOPEPTIDES, AMINO acids |
| مستخلص: |
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. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
Complementary Index |
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