RBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures

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dc.contributor.authorDomingues, Marco M.
dc.contributor.authorBianconi, M. Lucia
dc.contributor.authorBarbosa, Leandro R.S.
dc.contributor.authorSantiago, Patrícia S. [UNESP]
dc.contributor.authorTabak, Marcel
dc.contributor.authorCastanho, Miguel A.R.B.
dc.contributor.authorItri, Rosangela
dc.contributor.authorSantos, Nuno. C.
dc.contributor.institutionUniversidade de Lisboa
dc.contributor.institutionUniversidade Federal do Rio de Janeiro (UFRJ)
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-27T11:30:15Z
dc.date.available2014-05-27T11:30:15Z
dc.date.issued2013-08-27
dc.description.abstractrBPI21 belongs to the antimicrobial peptide and protein (AMP) family. It has high affinity for lipopolysaccharide (LPS), acting mainly against Gram-negative bacteria. This work intends to elucidate the mechanism of action of rBPI21 at the membrane level. Using isothermal titration calorimetry, we observed that rBPI21 interaction occurs only with negatively charged membranes (mimicking bacterial membranes) and is entropically driven. Differential scanning calorimetry shows that membrane interaction with rBPI21 is followed by an increase of rigidity on negatively charged membrane, which is corroborated by small angle X-ray scattering (SAXS). Additionally, SAXS data reveal that rBPI21 promotes the multilamellarization of negatively charged membranes. The results support the proposed model for rBPI21 action: first it may interact with LPS at the bacterial surface. This entropic interaction could cause the release of ions that maintain the packed structure of LPS, ensuring peptide penetration. Then, rBPI21 may interact with the negatively charged leaflets of the outer and inner membranes, promoting the interaction between the two bacterial membranes, ultimately leading to cell death. © 2013 Elsevier B.V.en
dc.description.affiliationInstituto de Medicina Molecular Faculdade de Medicina Universidade de Lisboa, Av. Prof. Egas Moniz, 1649-028 Lisbon
dc.description.affiliationPrograma de Biologia Estrutural Instituto de Bioquímica Médica Universidade Federal Do Rio de Janeiro, Rio de Janeiro, RJ
dc.description.affiliationInstituto de Física Universidade de São Paulo, São Paulo
dc.description.affiliationInstituto de Química de São Carlos Universidade de São Paulo, São Carlos, SP
dc.description.affiliationUniversidade Estadual Paulista Júlio de Mesquita Filho, Registro, SP
dc.description.affiliationUnespUniversidade Estadual Paulista Júlio de Mesquita Filho, Registro, SP
dc.format.extent2419-2427
dc.identifierhttp://dx.doi.org/10.1016/j.bbamem.2013.06.009
dc.identifier.citationBiochimica et Biophysica Acta - Biomembranes, v. 1828, n. 11, p. 2419-2427, 2013.
dc.identifier.doi10.1016/j.bbamem.2013.06.009
dc.identifier.issn0005-2736
dc.identifier.issn1879-2642
dc.identifier.lattes6705367010662087
dc.identifier.orcid0000-0002-6205-9441
dc.identifier.scopus2-s2.0-84882607788
dc.identifier.urihttp://hdl.handle.net/11449/76336
dc.identifier.wosWOS:000326143200008
dc.language.isoeng
dc.relation.ispartofBiochimica et Biophysica Acta: Biomembranes
dc.relation.ispartofjcr3.438
dc.relation.ispartofsjr1,495
dc.rights.accessRightsAcesso restrito
dc.sourceScopus
dc.subjectAMPen
dc.subjectLipopolysaccharideen
dc.subjectMembrane bindingen
dc.subjectMicrocalorimetryen
dc.subjectrBPI21en
dc.subjectSAXSen
dc.subjectlipopolysaccharideen
dc.subjectrecombinant bactericidal permeability increasing proteinen
dc.subjectapoptosisen
dc.subjectbacterial membraneen
dc.subjectcell structureen
dc.subjectdifferential scanning calorimetryen
dc.subjectGram negative bacteriumen
dc.subjectisothermal titration calorimetryen
dc.subjectlamellar bodyen
dc.subjectmembrane bindingen
dc.subjectmembrane leafleten
dc.subjectmembrane permeabilityen
dc.subjectmolecular interactionen
dc.subjectnonhumanen
dc.subjectphysical chemistryen
dc.subjectpriority journalen
dc.subjectprotein interactionen
dc.subjectprotein structureen
dc.subjectrigid multilamellar structureen
dc.subjectrigidityen
dc.subjectX ray crystallographyen
dc.titleRBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structuresen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
unesp.author.lattes6705367010662087[4]
unesp.author.orcid0000-0002-6205-9441[4]
unesp.campusUniversidade Estadual Paulista (Unesp), Faculdade de Ciências Agrárias do Vale do Ribeira, Registropt

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