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Hairpin Folding Behavior of Mixed α/β-Peptides in Aqueous Solution

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posted on 30.03.2011, 00:00 authored by George A. Lengyel, Rebecca C. Frank, W. Seth Horne
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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