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

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)3082-3090
Number of pages9
JournalChemistry - A European Journal
Volume9
Issue number13
DOIs
Publication statusPublished - Jul 7 2003

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Organic Chemistry

Fingerprint Dive into the research topics of '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'. Together they form a unique fingerprint.

  • Cite this