The fourth helical secondary structure of β-peptides: The (P)-28-helix of a β-hexapeptide consisting of (2R,3S)-3-amino-2-hydroxy acid residues

Karl Gademann; Andreas Häne; Magnus Rueping; Bernhard Jaun; Dieter Seebach

doi:10.1002/anie.200250290

The fourth helical secondary structure of β-peptides: The (P)-2₈-helix of a β-hexapeptide consisting of (2R,3S)-3-amino-2-hydroxy acid residues

Karl Gademann, Andreas Häne, Magnus Rueping, Bernhard Jaun, Dieter Seebach^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

88 Scopus citations

Abstract

Small change with great effect! An oligomer of α-hydroxy-β-amino acids folds into a right-handed helical structure (see picture) in MeOH; in contrast, the methyl analogue has a pleated sheet structure. Including this new helix, four different helical secondary structures of β-peptides have been discovered - a structural diversity that should allow the generation of elaborate proteomimetics.

Original language	English (US)
Pages (from-to)	1534-1537
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	42
Issue number	13
DOIs	https://doi.org/10.1002/anie.200250290
State	Published - Apr 4 2003
Externally published	Yes

Keywords

Amino acids
Beta-peptides
Conformational analysis
Peptidomimetics
Secondary structure

ASJC Scopus subject areas

Catalysis
General Chemistry

Access to Document

10.1002/anie.200250290

Cite this

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abstract = "Small change with great effect! An oligomer of α-hydroxy-β-amino acids folds into a right-handed helical structure (see picture) in MeOH; in contrast, the methyl analogue has a pleated sheet structure. Including this new helix, four different helical secondary structures of β-peptides have been discovered - a structural diversity that should allow the generation of elaborate proteomimetics.",

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AU - Jaun, Bernhard

AU - Seebach, Dieter

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KW - Conformational analysis

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