Artículo
Periodic bilayer organization in the complexes of Beta-2 Glycoprotein I with anionic lipid membranes
Oliveira, Rafael Gustavo
; Paolorossi Nucci, Mariana
; Cavalcanti, Leide Passos; Malfatti Gasperini, Antonio; Montich, Guillermo Gabriel
Fecha de publicación:
12/2021
Editorial:
Elsevier Science
Revista:
Colloids and Surfaces B: Biointerfaces
ISSN:
0927-7765
e-ISSN:
1873-4367
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
β2 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.
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Articulos(CIQUIBIC)
Articulos de CENTRO DE INVEST.EN QCA.BIOL.DE CORDOBA (P)
Articulos de CENTRO DE INVEST.EN QCA.BIOL.DE CORDOBA (P)
Citación
Oliveira, 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
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