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dc.contributor.authorGamba, Ilaria
dc.contributor.authorRama, Gustavo
dc.contributor.authorOrtega-Carrasco, Elisabeth
dc.contributor.authorBerardozzi, Roberto
dc.contributor.authorSánchez-Pedregal, Víctor M.
dc.contributor.authorDi Bari, Lorenzo
dc.contributor.authorMaréchal, Jean-Didier
dc.contributor.authorVázquez Sentís, Marco Eugenio
dc.contributor.authorVázquez López, Miguel
dc.date.accessioned2018-07-13T12:33:53Z
dc.date.available2018-07-13T12:33:53Z
dc.date.issued2016
dc.identifier.citationGamba, I., Rama, G., Ortega-Carrasco, E., Berardozzi, R., Sánchez-Pedregal, V., & Di Bari, L. et al. (2016). The folding of a metallopeptide. Dalton Transactions, 45(3), 881-885. doi: 10.1039/c5dt02797g
dc.identifier.issn1477-9226
dc.identifier.urihttp://hdl.handle.net/10347/17022
dc.description.abstractWe have applied solid-phase synthesis methods for the construction of tris(bipyridyl) peptidic ligands that coordinate Fe(II) ions with high affinity and fold into stable mononuclear metallopeptides. The main factors influencing the folding pathway and chiral control of the peptidic ligands around the metal ions have been studied both by experimental techniques (CD, UV-vis and NMR) and molecular modeling tools. Amongst the numerous molecular variables that have been studied, this study clearly illustrates how the chirality of a given set of aminoacids (proline in this case) of the peptide dictates the chirality of the metal center of the resulting metallopeptide. Moreover, the relatively hydrophobic peptidic models used in this work show that the most stable structures present reduced solvent contacts and, in counterpart, stabilize the cis configuration of the proline residues
dc.description.sponsorshipWe are thankful for the support given by the Spanish grants SAF2013-41943-R, CTQ2012-31341, CTQ2011-23336 and CTQ2013-49317-EXP; the ERDF and the European Research Council (Advanced Grant 340055); the Xunta de Galicia grants GRC2013-041 and PGIDIT08CSA-047209PR and the Generalitat de Catalunya grant 2009SGR68. Support of COST Action CM1105 is kindly acknowledged. G.R. thanks the INL for his PhD fellowship
dc.language.isoeng
dc.publisherRoyal Society of Chemistry
dc.rights© The Royal Society of Chemistry 2016
dc.titleThe folding of a metallopeptide
dc.typejournal article
dc.identifier.doi10.1039/C5DT02797G
dc.relation.publisherversionhttps://doi.org/10.1039/C5DT02797G
dc.type.hasVersionAM
dc.identifier.essn1477-9234
dc.rights.accessRightsopen access
dc.contributor.affiliationUniversidade de Santiago de Compostela. Centro de Investigación en Química Biolóxica e Materiais Moleculares
dc.contributor.affiliationUniversidade de Santiago de Compostela. Departamento de Química Inorgánica
dc.contributor.affiliationUniversidade de Santiago de Compostela. Departamento de Química Orgánica
dc.description.peerreviewedSI
dc.relation.projectIDinfo:eu-repo/grantAgreement/EC/FP7/340055
dc.relation.projectIDinfo:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/CTQ2013-49317/ES/EXPLORACION DE TERAPIAS ANTITUMORALES ALTERNATIVAS DIRIGIDAS A LAS MITOCONDRIAS
dc.relation.projectIDinfo:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/SAF2013-41943-R/ES/HERRAMIENTAS SINTETICAS EN QUIMICA BIOLOGICA. NUEVAS ESTRATEGIAS MOLECULARES PARA EL TRATAMIENTO Y DIAGNOSTICO DE CANCERES


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