rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures

Detalhes bibliográficos
Autor(a) principal: Domingues, Marco M.
Data de Publicação: 2013
Outros Autores: Bianconi, M. Lucia, Barbosa, Leandro R. S., Santiago, Patrícia S., Tabak, Marcel, Castanho, Miguel A. R. B., Itri, Rosangela, Santos, Nuno C.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10451/10691
Resumo: © 2013 Elsevier B.V. All rights reserved
id RCAP_7f77cc588ff2cd187354adf9b4fdc239
oai_identifier_str oai:repositorio.ul.pt:10451/10691
network_acronym_str RCAP
network_name_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository_id_str 7160
spelling rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structuresLipopolysaccharideAMPrBPI21Membrane bindingMicrocalorimetrySAXS© 2013 Elsevier B.V. All rights reservedrBPI21 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.rBPI21 was a kind gift from XOMA, Ltd. (Berkeley, CA). This work was partially supported by Fundação para a Ciência e a Tecnologia – Ministério do Ensino e Ciência (FCT-MEC, Portugal), by the FP7-PEOPLEIRSES project MEMPEPACROSS (European Union), and by the Brazilian funding agencies Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP), Fundação de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ) and Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq). MMD acknowledges FCT-MEC PhD fellowship SFRH/BD/41750/2007. RI and LRS Barbosa acknowledge CNPq for research fellowship. The authors are also in debt with Professors Francesco Spinozzi and Paolo Mariani (Università Politecnica delle Marche, Ancona, Italy), who developed and provided the GENFIT software.ElsevierRepositório da Universidade de LisboaDomingues, Marco M.Bianconi, M. LuciaBarbosa, Leandro R. S.Santiago, Patrícia S.Tabak, MarcelCastanho, Miguel A. R. B.Itri, RosangelaSantos, Nuno C.2014-03-06T11:25:01Z20132013-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10451/10691engBiochimica et Biophysica Acta 1828 (2013) 2419–24270006-3002http://dx.doi.org/10.1016/j.bbamem.2013.06.009metadata only accessinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-11-08T15:56:21Zoai:repositorio.ul.pt:10451/10691Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T21:34:37.879668Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures
title rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures
spellingShingle rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures
Domingues, Marco M.
Lipopolysaccharide
AMP
rBPI21
Membrane binding
Microcalorimetry
SAXS
title_short rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures
title_full rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures
title_fullStr rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures
title_full_unstemmed rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures
title_sort rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures
author Domingues, Marco M.
author_facet Domingues, Marco M.
Bianconi, M. Lucia
Barbosa, Leandro R. S.
Santiago, Patrícia S.
Tabak, Marcel
Castanho, Miguel A. R. B.
Itri, Rosangela
Santos, Nuno C.
author_role author
author2 Bianconi, M. Lucia
Barbosa, Leandro R. S.
Santiago, Patrícia S.
Tabak, Marcel
Castanho, Miguel A. R. B.
Itri, Rosangela
Santos, Nuno C.
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Repositório da Universidade de Lisboa
dc.contributor.author.fl_str_mv Domingues, Marco M.
Bianconi, M. Lucia
Barbosa, Leandro R. S.
Santiago, Patrícia S.
Tabak, Marcel
Castanho, Miguel A. R. B.
Itri, Rosangela
Santos, Nuno C.
dc.subject.por.fl_str_mv Lipopolysaccharide
AMP
rBPI21
Membrane binding
Microcalorimetry
SAXS
topic Lipopolysaccharide
AMP
rBPI21
Membrane binding
Microcalorimetry
SAXS
description © 2013 Elsevier B.V. All rights reserved
publishDate 2013
dc.date.none.fl_str_mv 2013
2013-01-01T00:00:00Z
2014-03-06T11:25:01Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10451/10691
url http://hdl.handle.net/10451/10691
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Biochimica et Biophysica Acta 1828 (2013) 2419–2427
0006-3002
http://dx.doi.org/10.1016/j.bbamem.2013.06.009
dc.rights.driver.fl_str_mv metadata only access
info:eu-repo/semantics/openAccess
rights_invalid_str_mv metadata only access
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv
_version_ 1799134241550761984