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X-ray crystallographic structure of α-helical peptide stabilized by hydrocarbon stapling at i,i + 1 positions
http://hdl.handle.net/10069/00040988
http://hdl.handle.net/10069/0004098899894e3a-9123-4535-a908-170b160a91c5
名前 / ファイル | ライセンス | アクション |
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IJMS22_5364.pdf (2.4 MB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2021-10-27 | |||||
タイトル | ||||||
タイトル | X-ray crystallographic structure of α-helical peptide stabilized by hydrocarbon stapling at i,i + 1 positions | |||||
言語 | ||||||
言語 | eng | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | peptide | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | α-helix | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | hydrocarbon stapling | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | ring-closingmetathesis | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | i,i + 1 staple | |||||
キーワード | ||||||
主題Scheme | Other | |||||
主題 | X-ray structure | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | journal article | |||||
著者 |
Makura, Yui
× Makura, Yui× Ueda, Atsushi× Kato, Takuma× Iyoshi, Akihiro× Higuchi, Mei× Doi, Mitsunobu× Tanaka, Masakazu |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | 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. | |||||
書誌情報 |
International Journal of Molecular Sciences 巻 22, 号 10, p. art. no. 5364, 発行日 2021-05-19 |
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出版者 | ||||||
出版者 | MDPI | |||||
EISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 14220067 | |||||
DOI | ||||||
関連タイプ | isIdenticalTo | |||||
識別子タイプ | DOI | |||||
関連識別子 | 10.3390/ijms22105364 | |||||
権利 | ||||||
権利情報 | © 2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). | |||||
著者版フラグ | ||||||
出版タイプ | VoR | |||||
出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
引用 | ||||||
内容記述タイプ | Other | |||||
内容記述 | International Journal of Molecular Sciences, 22(10), art. no. 5364; 2021 |