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dc.creatorKlug, Joaquín-
dc.creatorMasone, Diego Fernando-
dc.creatordel Popolo, Mario Gabriel-
dc.date2018-06-19T19:21:07Z-
dc.date2018-06-19T19:21:07Z-
dc.date2017-06-
dc.date2018-06-13T16:54:16Z-
dc.date.accessioned2019-04-29T15:43:35Z-
dc.date.available2019-04-29T15:43:35Z-
dc.date.issued2018-06-19T19:21:07Z-
dc.date.issued2018-06-19T19:21:07Z-
dc.date.issued2017-06-
dc.date.issued2018-06-13T16:54:16Z-
dc.identifierKlug, Joaquín; Masone, Diego Fernando; del Popolo, Mario Gabriel; Molecular-level insight into the binding of arginine to a zwitterionic Langmuir monolayer; Royal Society of Chemistry; RSC Advances; 7; 49; 6-2017; 30862-30869-
dc.identifier2046-2069-
dc.identifierhttp://hdl.handle.net/11336/49420-
dc.identifierCONICET Digital-
dc.identifierCONICET-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/300421-
dc.descriptionSolutions of the cationic amino-acid arginine (Arg+) in contact with a phospholipid monolayer are investigated by molecular dynamics simulations. The results show that Arg+ binds strongly to the lipid/water interface, with adsorption free-energies ranging from -43.8 to -22.2 kJ mol-1, depending on the amino-acids concentration. The large binding energies are attributed to hydrogen bonding between the charged moieties Arg+ and the phosphate and carbonyl groups of the phospholipids, that compensate for changes in the levels of hydration upon adsorption. We show that a concentrated layer of Arg+, tightly bound to the interface, has little effect on the compression isotherm and the lateral mechanical properties of the monolayer, while having a substantial impact on the interfacial electrostatic potential and the lateral mobility of the lipids. These effects are readily explained in terms of the arrangement that the amino-acids adopt when bound to the monolayer.-
dc.descriptionFil: Klug, Joaquín. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Argentina. Queen's University Belfast; Reino Unido. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina-
dc.descriptionFil: Masone, Diego Fernando. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mendoza. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos. Universidad Nacional de Cuyo. Facultad de Cienicas Médicas. Instituto de Histología y Embriología de Mendoza Dr. Mario H. Burgos; Argentina-
dc.descriptionFil: del Popolo, Mario Gabriel. Universidad Nacional de Cuyo. Facultad de Ciencias Exactas y Naturales; Argentina-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherRoyal Society of Chemistry-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://xlink.rsc.org/?DOI=C7RA05359B-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1039/C7RA05359B-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://pubs.rsc.org/en/Content/ArticleLanding/2017/RA/C7RA05359B#!divAbstract-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.rightshttps://creativecommons.org/licenses/by/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.subjectMOLECULAR DYNAMICS-
dc.subjectLANGMUIR MONOLAYER-
dc.subjectARGININE-
dc.subjectFREE ENERGY-
dc.subjectOtras Ciencias Biológicas-
dc.subjectCiencias Biológicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.titleMolecular-level insight into the binding of arginine to a zwitterionic Langmuir monolayer-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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