New helical foldamers: Heterogeneous backbones with 1:2 and 2:1 α:β-amino acid residue patterns

Margaret A. Schmitt, Soo Hyuk Choi, Ilia A. Guzei, Samuel H. Gellman

Research output: Contribution to journalArticle

76 Citations (Scopus)

Abstract

Foldamers, oligomers with strong folding propensities, are subjects of growing interest because such compounds offer unique scaffolds for the development of molecular function. We report two new foldamer classes, oligopeptides with regular 1:2 or 2:1 patterns of α- and β-amino acid residues. Two distinct helical conformations are detected via 2D NMR in methanol for each backbone. One of the helices for each backbone is characterized via X-ray crystallography.

Original languageEnglish
Pages (from-to)4538-4539
Number of pages2
JournalJournal of the American Chemical Society
Volume128
Issue number14
DOIs
Publication statusPublished - 2006 Apr 12

Fingerprint

Oligopeptides
X ray crystallography
X Ray Crystallography
Oligomers
Scaffolds
Methanol
Conformations
Amino acids
Nuclear magnetic resonance
Amino Acids

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

Schmitt, Margaret A. ; Choi, Soo Hyuk ; Guzei, Ilia A. ; Gellman, Samuel H. / New helical foldamers : Heterogeneous backbones with 1:2 and 2:1 α:β-amino acid residue patterns. In: Journal of the American Chemical Society. 2006 ; Vol. 128, No. 14. pp. 4538-4539.
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New helical foldamers : Heterogeneous backbones with 1:2 and 2:1 α:β-amino acid residue patterns. / Schmitt, Margaret A.; Choi, Soo Hyuk; Guzei, Ilia A.; Gellman, Samuel H.

In: Journal of the American Chemical Society, Vol. 128, No. 14, 12.04.2006, p. 4538-4539.

Research output: Contribution to journalArticle

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