Please use this identifier to cite or link to this item: https://hdl.handle.net/11000/4783
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dc.contributor.authorZamora Carreras, Héctor-
dc.contributor.authorMaestro García-Donas, Beatriz-
dc.contributor.authorStrandberg, Erik-
dc.contributor.authorUlrich, Anne S.-
dc.contributor.authorSanz, Jesús M.-
dc.contributor.authorJiménez, M. Ángeles-
dc.contributor.otherDepartamentos de la UMH::Bioquímica y Biología Moleculares
dc.date.accessioned2018-07-16T13:05:33Z-
dc.date.available2018-07-16T13:05:33Z-
dc.date.created2018-03-15-
dc.date.issued2018-07-16-
dc.identifier.issn0947-6539-
dc.identifier.issn1521-3765-
dc.identifier.urihttp://hdl.handle.net/11000/4783-
dc.description.abstractCholine-binding repeats (CBRs) are ubiquitous sequences with a b-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 bhairpin conformation in aqueous solution but is reversibly transformed into an amphipathic a-helix in the presence of detergent micelles. With the aim of understanding the factors responsible for this unusual b-hairpin to a-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 b-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 peptidesen
dc.description.sponsorshipThis work was supported by the Spanish MINECO grants (co-financed by European FEDER funds): CTQ2017-84371-P,-
dc.description.sponsorshipThis work was supported by the Spanish MINECO grants CTQ2014-52633-P-
dc.description.sponsorshipThis work was supported by the Spanish MINECO grants BIO2016-79323-R-
dc.description.sponsorshipThis work was supported by the German Helmholtz Gemeinschaft. H. Zamora-Carreras was a recipient of a FPI scholarship (BES-2012-057717)-
dc.description.sponsorshipGermany was financed by the Spanish MINECO short stay grant EEBB-I-14-08805.-
dc.formatapplication/pdfes
dc.format.extent43es
dc.language.isoenges
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.subject.otherCiencias puras y naturales::57 - Biología::576 - Biología celular y subcelular. Citologíaes
dc.titleRoles of Amphipathicity and Hydrophobicity in the Micelle-Driven Structural Switch of a 14-mer Peptide Core from a Choline-Binding Repeates
dc.typeinfo:eu-repo/semantics/articlees
dc.identifier.doi10.1002/chem.201704802-
dc.relation.publisherversionhttps://doi.org/ 10.1002/chem.201704802-
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