An extended planar C5 conformation and a 310-helical structure of peptide foldamer composed of diverse α-ethylated α,α-disubstituted α-amino acids

Masakazu Tanaka, Shin Nishimura, Makoto Oba, Yosuke Demizu, Masaaki Kurihara, Hiroshi Suemune

研究成果: Contribution to journalArticle査読

38 被引用数 (Scopus)

抄録

Optically active peptide foldamers Tfa-[(S)-(αEt)Leu]-[(S)-(αEt)Nva]-Deg-[(S)-(αEt)Nle]-OEt (10) and Tfa-[(S)-(αEt)Val]-[(S)-(αEt)Leu]- [(S)-(αEt)-Nva]-Deg-[(S)-(αEt)Nle]-OEt (11) composed of diverse α-ethylated α,α-disubstituted α-amino acids were synthesized. The dominant conformation of these peptides in solution was an unusual, fully extended planar conformation, and that in the crystal state was both right-handed (P) and left-handed (M) 310-helical structures in 10 and a P 310-helical structure in 11, respectively. The preferred planar C5 conformation of the peptides prepared from chiral α-ethylated α,α-disubstituted α-amino acids was drastically different from the 310-helical structure of the peptides prepared from chiral α-methylated α,α-disubstituted α-amino acids.

本文言語英語
ページ(範囲)3082-3090
ページ数9
ジャーナルChemistry - A European Journal
9
13
DOI
出版ステータス出版済み - 7 7 2003

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Organic Chemistry

フィンガープリント 「An extended planar C<sub>5</sub> conformation and a 3<sub>10</sub>-helical structure of peptide foldamer composed of diverse α-ethylated α,α-disubstituted α-amino acids」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

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