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dc.contributor.authorZamora-Carreras, H.-
dc.contributor.authorMaestro, Beatriz-
dc.contributor.authorStrandberg, E.-
dc.contributor.authorUlrich, A.S.-
dc.contributor.authorSanz, J.M.-
dc.contributor.authorJiménez, M. Angeles-
dc.identifierdoi: 10.1002/chem.201500447-
dc.identifierissn: 1521-3765-
dc.identifier.citationChemistry - A European Journal 21: 8076-8089 (2015)-
dc.description.abstract© 2014 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. Choline-binding modules (CBMs) have a ββ-solenoid structure composed of choline-binding repeats (CBR), which consist of a β-hairpin followed by a short linker. To find minimal peptides that are able to maintain the CBR native structure and to evaluate their remaining choline-binding ability, we have analysed the third β-hairpin of the CBM from the pneumococcal LytA autolysin. Circular dichroism and NMR data reveal that this peptide forms a highly stable native-like β-hairpin both in aqueous solution and in the presence of trifluoroethanol, but, strikingly, the peptide structure is a stable amphipathic α-helix in both zwitterionic (dodecylphosphocholine) and anionic (sodium dodecylsulfate) detergent micelles, as well as in small unilamellar vesicles. This β-hairpin to α-helix conversion is reversible. Given that the β-hairpin and α-helix differ greatly in the distribution of hydrophobic and hydrophilic side chains, we propose that the amphipathicity is a requirement for a peptide structure to interact and to be stable in micelles or lipid vesicles. To our knowledge, this >chameleonic> behaviour is the only described case of a micelle-induced structural transition between two ordered peptide structures.-
dc.publisherJohn Wiley & Sons-
dc.titleMicelle-triggered β-hairpin to α-helix transition in a 14-residue peptide from a choline-binding repeat of the pneumococcal autolysin LytA-
dc.description.versionPeer Reviewed-
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