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Mapping a protein recognition centre with chiral photoactive ligands. An integrated approach combining photophysics, reactivity, proteomics and molecular dynamics simulation studies

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Mapping a protein recognition centre with chiral photoactive ligands. An integrated approach combining photophysics, reactivity, proteomics and molecular dynamics simulation studies

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dc.contributor.author Limones-Herrero, Daniel es_ES
dc.contributor.author Pérez Ruiz, Raul es_ES
dc.contributor.author Lence, Emilio es_ES
dc.contributor.author Gonzalez-Bello, Concepcion es_ES
dc.contributor.author Miranda Alonso, Miguel Ángel es_ES
dc.contributor.author Jiménez Molero, María Consuelo es_ES
dc.date.accessioned 2020-10-22T03:32:11Z
dc.date.available 2020-10-22T03:32:11Z
dc.date.issued 2017-04-01 es_ES
dc.identifier.issn 2041-6520 es_ES
dc.identifier.uri http://hdl.handle.net/10251/152805
dc.description.abstract [EN] A multidisciplinary strategy to obtain structural information on the intraprotein region is described here. As probe ligands, (S)- and (R)-CPFMe (the methyl esters of the chiral drug carprofen) have been selected, while bovine 1-acid glycoprotein (BAAG) has been chosen as biological host. The procedure involves separate irradiation of the BAAG/(S)-CPFMe and BAAG/(R)-CPFMe complexes, coupled with fluorescence, laser flash photolysis, proteomic analysis, docking and molecular dynamic simulations. Thus, irradiation of the BAAG/CPFMe complexes at  = 320 nm, was followed by fluorescence spectroscopy. The intensity of the emission band obtained after irradiation indicated photodehalogenation, whereas its structureless shape suggested covalent binding of the resulting radical CBZMe● to the biopolymer. After gel filtration chromatography, the spectra still displayed emission, in agreement with covalent attachment of CBZMe● to BAAG. Stereodifferentiation was observed in this process. After trypsin digestion and ESI-MS/MS, incorporation of CBZMe was detected at Phe68. Docking and molecular dynamics simulation studies, which were carried out using a homology model of BAAG, reveal that the closer proximity of the aromatic moiety of the (S)- enantiomer to the phenyl group of Phe68 would be responsible for the experimentally observed more effective chemical modification of the protein. The proposed tridimensional structure of BAAG covalently modified by the two enantiomers is also provided. In principle, this approach can be extended to a variety of protein/ligand complexes. es_ES
dc.description.sponsorship Financial support from the Spanish Ministry of Economy and Competitiveness (CTQ2013-47872-C2-1-P, SAF2013-42899-R, BES-2011-043706), Generalitat Valenciana (PROMETEOII/2013/005), Instituto de Salud Carlos III (RD12/0013/0009), Xunta de Galicia (GRC2013-041), the Conselleria de Cultura, Educacion e Ordenacion Universitaria (Centro singular de investigacion de Galicia accreditation 2016-2019, ED431G/09) and the European Regional Development Fund (ERDF) is gratefully acknowledged. E. L. thanks the Xunta de Galicia for a postdoctoral fellowship. We are grateful to the Centro de Supercomputacion de Galicia (CESGA) for use of the Finis Terrae II supercomputer. The proteomic analysis was performed in the proteomics facility of SCSIE University of Valencia that belongs to ProteoRed PRB2-ISCIII and is supported by grant PT13/0001, of the PE I+D+i 2013-2016, funded by ISCIII and FEDER es_ES
dc.language Inglés es_ES
dc.publisher The Royal Society of Chemistry es_ES
dc.relation.ispartof Chemical Science es_ES
dc.rights Reconocimiento - No comercial (by-nc) es_ES
dc.subject.classification QUIMICA ORGANICA es_ES
dc.subject.classification QUIMICA ANALITICA es_ES
dc.title Mapping a protein recognition centre with chiral photoactive ligands. An integrated approach combining photophysics, reactivity, proteomics and molecular dynamics simulation studies es_ES
dc.type Artículo es_ES
dc.identifier.doi 10.1039/c6sc04900a es_ES
dc.relation.projectID info:eu-repo/grantAgreement/Xunta de Galicia//ED431G%2F09/ es_ES
dc.relation.projectID info:eu-repo/grantAgreement/UV//PT13%2F0001/ es_ES
dc.relation.projectID info:eu-repo/grantAgreement/MINECO//SAF2013-42899-R/ES/DESARROLLO DE NUEVOS ANTIBIOTICOS PARA EL TRATAMIENTO DE INFECCIONES BACTERIANAS RESISTENTES: METABOLISMO, RESISTENCIA Y COMUNICACION CELULA-CELULA/ es_ES
dc.relation.projectID info:eu-repo/grantAgreement/Xunta de Galicia//GRC2013-041/ es_ES
dc.relation.projectID info:eu-repo/grantAgreement/MINECO//RD12%2F0013%2F0009/ es_ES
dc.relation.projectID info:eu-repo/grantAgreement/GVA//PROMETEOII%2F2013%2F005/ES/ESPECIES FOTOACTIVAS Y SU INTERACCION CON BIOMOLECULAS/ es_ES
dc.relation.projectID info:eu-repo/grantAgreement/MICINN//BES-2011-043706/ES/BES-2011-043706/ es_ES
dc.relation.projectID info:eu-repo/grantAgreement/MINECO//CTQ2013-47872-C2-1-P/ES/METABOLITOS FOTOACTIVOS/ es_ES
dc.rights.accessRights Abierto es_ES
dc.contributor.affiliation Universitat Politècnica de València. Departamento de Química - Departament de Química es_ES
dc.description.bibliographicCitation Limones-Herrero, D.; Pérez Ruiz, R.; Lence, E.; Gonzalez-Bello, C.; Miranda Alonso, MÁ.; Jiménez Molero, MC. (2017). Mapping a protein recognition centre with chiral photoactive ligands. An integrated approach combining photophysics, reactivity, proteomics and molecular dynamics simulation studies. Chemical Science. 8(4):2621-2628. https://doi.org/10.1039/c6sc04900a es_ES
dc.description.accrualMethod S es_ES
dc.relation.publisherversion https://doi.org/10.1039/c6sc04900a es_ES
dc.description.upvformatpinicio 2621 es_ES
dc.description.upvformatpfin 2628 es_ES
dc.type.version info:eu-repo/semantics/publishedVersion es_ES
dc.description.volume 8 es_ES
dc.description.issue 4 es_ES
dc.identifier.pmid 28553497 es_ES
dc.identifier.pmcid PMC5431658 es_ES
dc.relation.pasarela S\340352 es_ES
dc.contributor.funder Xunta de Galicia es_ES
dc.contributor.funder Generalitat Valenciana es_ES
dc.contributor.funder Universitat de València es_ES
dc.contributor.funder Ministerio de Economía y Competitividad es_ES
dc.contributor.funder Ministerio de Ciencia e Innovación es_ES
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