Abstract
A comparative monolayer and infrared study of analogues of gramicidin A containing either tyrosines or naphthylalanines instead of tryptophans indicates that the nature of the aromatic residues influences the favoured conformation of the peptides. Polar residues favour the single stranded ΠDL helix while non polar residues favour the double stranded helix. For partly tryptophan to naphthylalanine substituted analogues the positions of the substitutions orientate the favored conformation. The nature of these substitutions may also modify the peptide-lipid interactions.
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Correspondence to: F. Heitz
Chemical structures of the gramicidin A analogues mentioned in this paper. The differences from gramicidin A are underlined. GM−: GT:
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Van Mau, N., Bonnet, B., Benayad, A. et al. The conformation of linear gramicidin is sequence dependent. Eur Biophys J 22, 447–452 (1994). https://doi.org/10.1007/BF00180165
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DOI: https://doi.org/10.1007/BF00180165