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

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

Research output: Contribution to journalArticle

Abstract

Optically active peptide foldamers Tfa-[(S)-(alphaEt)Leu]-[(S)-(alphaEt)Nva]-Deg-[(S)-(alphaEt)Nle]-OEt (10) and Tfa-[(S)-(alphaEt)Val]-[(S)-(alphaEt)Leu]-[(S)-(alphaEt)Nva]-Deg-[(S)-(alphaEt)Nle]-OEt (11) composed of diverse alpha-ethylated alpha,alpha-disubstituted alpha-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) 3(10)-helical structures in 10 and a P 3(10)-helical structure in 11, respectively. The preferred planar C(5) conformation of the peptides prepared from chiral alpha-ethylated alpha,alpha-disubstituted alpha-amino acids was drastically different from the 3(10)-helical structure of the peptides prepared from chiral alpha-methylated alpha,alpha-disubstituted alpha-amino acids.

Original languageEnglish
Pages (from-to)3082-3090
Number of pages9
JournalChemistry (Weinheim an der Bergstrasse, Germany)
Volume9
Issue number13
Publication statusPublished - Jul 7 2003

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All Science Journal Classification (ASJC) codes

  • Chemistry(all)

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