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dc.contributor.authorZamora-Carreras, H.es_ES
dc.contributor.authorMaestro, Beatrizes_ES
dc.contributor.authorStrandberg, E.es_ES
dc.contributor.authorUlrich, A.S.es_ES
dc.contributor.authorSanz, J.M.es_ES
dc.contributor.authorJiménez, M. Angeleses_ES
dc.date.accessioned2018-03-22T11:09:51Z-
dc.date.available2018-03-22T11:09:51Z-
dc.date.issued2018-
dc.identifier.citationChemistry (2018) doi:10.1002/chem.201704802-
dc.identifier.urihttp://hdl.handle.net/10261/162693-
dc.description.abstractCholine‐binding repeats (CBRs) are ubiquitous sequences with a β‐hairpin core that are found in the surface proteins of several microorganisms such as S. pneumoniae (pneumococcus). Previous studies on a 14‐mer CBR sequence derived from the pneumoccal LytA autolysin (LytA239–252 peptide) have demonstrated a switch behaviour for this peptide, so that it acquires a stable, native‐like β‐hairpin conformation in aqueous solution but is reversibly transformed into an amphipathic α‐helix in the presence of detergent micelles. With the aim of understanding the factors responsible for this unusual β‐hairpin to α‐helix transition, and to specifically assess the role of peptide hydrophobicity and helical amphipathicity in the process, we designed a series of LytA239–252 variants affecting these two parameters and studied their interaction with dodecylphosphocholine (DPC) micelles by solution NMR, circular dichroism and fluorescence spectroscopies. Our results indicate that stabilising cross‐strand interactions become essential for β‐hairpin stability in the absence of optimal turn sequences. Moreover, both amphipathicity and hydrophobicity display comparable importance for helix stabilisation of CBR‐derived peptides in micelles, indicating that these sequences represent a novel class of micelle/membrane‐interacting peptides.es_ES
dc.description.sponsorshipThis work was supported by the Spanish MINECO grants (co-financed by European FEDER funds): CTQ2017-84371-P, CTQ2014-52633-P, BIO2016-79323-R and BIO2013-47684-R; and by the German Helmholtz Gemeinschaft. H. Zamora-Carreras was a recipient of a FPI scholarship (BES-2012-057717), and his stay at KIT, Germany was financed by the Spanish MINECO short stay grant EEBB-I-14-08805. We thank Dr. Jochen B rck and his team for the CD facilities at IBG2. We also thank M. Garz n and R. Aldomar for excellent technical assistance.es_ES
dc.language.isoenges_ES
dc.publisherWiley-VCHes_ES
dc.relationMINECO/ICTI2013-2016/CTQ2014-52633-Pes_ES
dc.rightsopenAccesses_ES
dc.subjectMicelleses_ES
dc.subjectPeptideses_ES
dc.subjectProtein foldinges_ES
dc.subjectProtein Structureses_ES
dc.subjectStructural biologyes_ES
dc.titleRoles of amphipathicity and hydrophobicity in the micelle-driven structural switch of a 14-mer peptide core from a choline-binding repeates_ES
dc.typeartículoes_ES
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttps://onlinelibrary.wiley.com/doi/epdf/10.1002/chem.201704802es_ES
dc.identifier.e-issn1521-3765 doi:10.1002/chem.201704802-
dc.contributor.funderMinisterio de Economía y Competitividad (España)es_ES
dc.relation.csices_ES
oprm.item.hasRevisionno ko 0 false*
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
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