dc.creatorOliveira, Rafael Gustavo
dc.creatorPaolorossi Nucci, Mariana
dc.creatorCavalcanti, Leide Passos
dc.creatorMalfatti Gasperini, Antonio
dc.creatorMontich, Guillermo Gabriel
dc.date2021-12
dc.date.accessioned2023-08-31T00:06:44Z
dc.date.available2023-08-31T00:06:44Z
dc.identifierhttp://hdl.handle.net/11336/184947
dc.identifierOliveira, Rafael Gustavo; Paolorossi Nucci, Mariana; Cavalcanti, Leide Passos; Malfatti Gasperini, Antonio; Montich, Guillermo Gabriel; Periodic bilayer organization in the complexes of Beta-2 Glycoprotein I with anionic lipid membranes; Elsevier Science; Colloids and Surfaces B: Biointerfaces; 208; 12-2021; 1-7
dc.identifier0927-7765
dc.identifier1873-4367
dc.identifierCONICET Digital
dc.identifierCONICET
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8543110
dc.descriptionβ2 glycoprotein I (β2GPI) is a soluble protein that participates in blood coagulation, clearance of apoptotic bodies and generation of antigens in antiphospholipid syndrome among many other functions. We studied the aggregates formed by β2GPI with the anionic phospholipids palmitoyloleoylphosphatidyl glycerol, dimyristoylphosphatidyl glycerol, dipalmitoylphosphatidyl glycerol and cardiolipin using small angle X-ray scattering. The complexes obtained in a medium containing 0.01 M NaCl showed Bragg peaks up to the sixth order in a well-defined integer sequence indicating the presence of a lamellar stacking with a periodicity of 17.8 nm and with largely reduced membrane fluctuations. Modeling the complex signal allowed us to conclude that the coherence length was only two bilayers and that about 15% of the total surface was actually stacked. The space between bilayers allows accommodating an extended β2GPI molecule making a bridge between the interacting bilayers. The interactions between membranes mediated by β2GPI was favored when the membranes were in the liquid crystalline state.
dc.descriptionFil: Oliveira, Rafael Gustavo. Universidad Nacional de Córdoba; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
dc.descriptionFil: Paolorossi Nucci, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina. Universidad Nacional de Córdoba; Argentina
dc.descriptionFil: Cavalcanti, Leide Passos. Isis Neutron And Muon Source; Reino Unido
dc.descriptionFil: Malfatti Gasperini, Antonio. Brazilian Synchrotron Light Laboratory; Brasil
dc.descriptionFil: Montich, Guillermo Gabriel. Universidad Nacional de Córdoba; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
dc.formatapplication/pdf
dc.formatapplication/pdf
dc.languageeng
dc.publisherElsevier Science
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.colsurfb.2021.112118
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0927776521005622
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subjectANIONIC PHOSPHOLIPIDS
dc.subjectBETA-2 GLYCOPROTEIN 1
dc.subjectPROTEIN LIPID MEMBRANE INTERACTION
dc.subjectSAXS
dc.subjecthttps://purl.org/becyt/ford/1.6
dc.subjecthttps://purl.org/becyt/ford/1
dc.titlePeriodic bilayer organization in the complexes of Beta-2 Glycoprotein I with anionic lipid membranes
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:ar-repo/semantics/artículo
dc.typeinfo:eu-repo/semantics/publishedVersion


Este ítem pertenece a la siguiente institución