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Unusual β-sheet periodicity in small cyclic peptides

Abstract

Cyclic peptide homologs of gramicidin S containing 6, 8, 10, 12, 14 and 16 residues were synthesized and characterized using circular dichroism (CD) and 1H NMR spectroscopy. Based on the three-dimensional structures generated from these data we have found strong evidence of a periodic sequence-length dependence on β-sheet content. In particular, peptides of length 6, 10 and 14 residues exhibit a high β-sheet content, while peptides of 8, 12 and 16 residues appear to exist as random coils. This unusual β-sheet periodicity may have important implications in our understanding of β-sheet formation and in the design of constrained β-sheet and β-hairpin mimics.

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Correspondence to David S. Wishart.

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Gibbs, A., Kondejewski, L., Gronwald, W. et al. Unusual β-sheet periodicity in small cyclic peptides. Nat Struct Mol Biol 5, 284–288 (1998). https://doi.org/10.1038/nsb0498-284

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