Molecular features of nonionic detergents involved in the binding kinetics and solubilization efficiency, as studied in model (Langmuir films) and biological (Erythrocytes) membranes

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dc.contributor.authorCasadei, Bruna Renata [UNIFESP]
dc.contributor.authorDomingues, Cleyton Crepaldi
dc.contributor.authorClop, Eduardo M.
dc.contributor.authorCouto, Veronica Muniz
dc.contributor.authorPerillo, Maria Angelica
dc.contributor.authorPaula, Eneida de
dc.date.accessioned2018-07-26T12:18:40Z
dc.date.available2018-07-26T12:18:40Z
dc.date.issued2018
dc.description.abstractThe effect of the nonionic detergents Brij-98 and Brij-58 over human erythrocytes was studied through quantitative hemolysis and in Langmuir films. Hemolytic tests revealed that Brijs are stronger membrane solubilizers than Triton X-100 (TX-100), with effective detergent/lipid ratios of 0.18 and 0.37 for Brij-98 and Brij-58, respectively. Experiments with Langmuir films provided significant information on the kinetics and thermodynamics of detergent-membrane interaction. The adsorption (k(a)) and desorption (k(d)) rate constants of Brijs were lower than those of TX-100. In the case of k(a), that is probably due to their larger hydrophilic head (with twice (20) the oxyethylene units of TX-100). As for the thermodynamic binding constant, the linear and longer hydrophobic acyl chains of Brijs favor their stabilization in-between the lipids, through London van der Waals forces. Consequently, K-b,K-m values of Brij-98 (12,500 M-1) and Brij-58 (19,300 M-1) resulted higher than TX-100 (7500 M-1), in agreement with results from the hemolytic tests. Furthermore, Brij-58 binds with higher affinity than Brij-98 to bilayers and monolayers, despite its shorter (palmitic) hydrocarbon chain, showing that unsaturation restrains the detergent insertion into these environments. Our results provide significant information about the mechanism of interaction between Brijs and membranes, supporting their distinct solubilization effect. (C) 2018 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniv Estadual Campinas UNICAMP, Inst Biol, Dept Bioquim Biol & Tecidual, Campinas, SP, Brazil
dc.description.affiliationUniv Fed Sao Paulo, Dept Biofis, Sao Paulo, SP, Brazil
dc.description.affiliationGeorge Washington Univ, Dept Med, Washington, DC USA
dc.description.affiliationUniv Nacl Cordoba, Fac Ciencias Exactas Fis & Nat, Dept Quim, Catedra Quim Biol, Cordoba, Argentina
dc.description.affiliationUniv Nacl Cordoba, CONICET, Cordoba, Argentina
dc.description.affiliationUnifespUniv Fed Sao Paulo, Dept Biofis, Sao Paulo, SP, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipCapes (Brazil)
dc.description.sponsorshipMincyt
dc.description.sponsorshipSeCyT-Universidad Nacional de Cordoba
dc.description.sponsorshipCONICET
dc.description.sponsorshipFoncyt (Argentina)
dc.description.sponsorshipCNPq
dc.description.sponsorshipCAPES
dc.description.sponsorshipIDCNPq: 479993/2011-4
dc.description.sponsorshipIDCNPq: 308621/2013-1
dc.format.extent152-160
dc.identifierhttp://dx.doi.org/10.1016/j.colsurfb.2018.03.012
dc.identifier.citationColloids And Surfaces B-Biointerfaces. Amsterdam, v. 166, p. 152-160, 2018.
dc.identifier.doi10.1016/j.colsurfb.2018.03.012
dc.identifier.issn0927-7765
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/46000
dc.identifier.wosWOS:000432505900019
dc.language.isoeng
dc.publisherElsevier Science Bv
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectErythrocyte membranesen
dc.subjectSolubilizationen
dc.subjectMonolayersen
dc.subjectNonionic detergentsen
dc.subjectBrijen
dc.titleMolecular features of nonionic detergents involved in the binding kinetics and solubilization efficiency, as studied in model (Langmuir films) and biological (Erythrocytes) membranesen
dc.typeinfo:eu-repo/semantics/article
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