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

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorDomingues, Marco M.
dc.creatorBianconi, M. Lucia
dc.creatorBarbosa, Leandro R.S.
dc.creatorSantiago, Patrícia S.
dc.creatorTabak, Marcel
dc.creatorCastanho, Miguel A.R.B.
dc.creatorItri, Rosangela
dc.creatorSantos, Nuno. C.
dc.date2014-05-27T11:30:15Z
dc.date2016-10-25T18:52:59Z
dc.date2014-05-27T11:30:15Z
dc.date2016-10-25T18:52:59Z
dc.date2013-08-27
dc.date.accessioned2017-04-06T02:36:13Z
dc.date.available2017-04-06T02:36:13Z
dc.identifierBiochimica et Biophysica Acta - Biomembranes, v. 1828, n. 11, p. 2419-2427, 2013.
dc.identifier0005-2736
dc.identifier1879-2642
dc.identifierhttp://hdl.handle.net/11449/76336
dc.identifierhttp://acervodigital.unesp.br/handle/11449/76336
dc.identifier10.1016/j.bbamem.2013.06.009
dc.identifierWOS:000326143200008
dc.identifier2-s2.0-84882607788
dc.identifierhttp://dx.doi.org/10.1016/j.bbamem.2013.06.009
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/897036
dc.descriptionrBPI21 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.
dc.languageeng
dc.relationBiochimica et Biophysica Acta: Biomembranes
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectAMP
dc.subjectLipopolysaccharide
dc.subjectMembrane binding
dc.subjectMicrocalorimetry
dc.subjectrBPI21
dc.subjectSAXS
dc.subjectlipopolysaccharide
dc.subjectrecombinant bactericidal permeability increasing protein
dc.subjectapoptosis
dc.subjectbacterial membrane
dc.subjectcell structure
dc.subjectdifferential scanning calorimetry
dc.subjectGram negative bacterium
dc.subjectisothermal titration calorimetry
dc.subjectlamellar body
dc.subjectmembrane binding
dc.subjectmembrane leaflet
dc.subjectmembrane permeability
dc.subjectmolecular interaction
dc.subjectnonhuman
dc.subjectphysical chemistry
dc.subjectpriority journal
dc.subjectprotein interaction
dc.subjectprotein structure
dc.subjectrigid multilamellar structure
dc.subjectrigidity
dc.subjectX ray crystallography
dc.titleRBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures
dc.typeOtro


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