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Updated: Jun 4, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Hairpin folding behavior of mixed α/β-peptides in aqueous solution
George A Lengyel1, Rebecca C Frank, W Seth Horne
1Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA.
Abstract:
The invention of new strategies for the design of protein-mimetic oligomers that manifest the folding encoded in natural amino acid sequences is a significant challenge. In contrast to the α-helix, mimicry of protein β-sheets is less understood. We report here the aqueous folding behavior of a prototype α-peptide hairpin model sequence varied at cross-strand positions by incorporation of 16 different β-amino acid monomers. Our results provide a folding propensity scale for β-residues in a protein β-sheet context as well as high-resolution structures of several mixed-backbone α/β-peptide hairpins in water.
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