Publicação
rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures
| Resumo: | rBPI21 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. |
|---|---|
| Autores principais: | Domingues, Marco M. |
| Outros Autores: | Bianconi, M. Lucia; Barbosa, Leandro R. S.; Santiago, Patrícia S.; Tabak, Marcel; Castanho, Miguel A. R. B.; Itri, Rosangela; Santos, Nuno C. |
| Assunto: | Lipopolysaccharide AMP rBPI21 Membrane binding Microcalorimetry SAXS |
| Ano: | 2013 |
| País: | Portugal |
| Tipo de documento: | artigo |
| Tipo de acesso: | acesso restrito |
| Instituição associada: | Universidade de Lisboa |
| Idioma: | inglês |
| Origem: | Repositório da Universidade de Lisboa |
| _version_ | 1865920822288318464 |
|---|---|
| author | Domingues, Marco M. |
| 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 |
| author_facet | Domingues, Marco M. 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. 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 |
| contributor_name_str_mv | Repositório Científico de Acesso Aberto da ULisboa |
| country_str | PT |
| creators_json_str | [{\"Person.name\":\"Domingues, Marco M.\"},{\"Person.name\":\"Bianconi, M. Lucia\"},{\"Person.name\":\"Barbosa, Leandro R. S.\"},{\"Person.name\":\"Santiago, Patrícia S.\"},{\"Person.name\":\"Tabak, Marcel\"},{\"Person.name\":\"Castanho, Miguel A. R. B.\"},{\"Person.name\":\"Itri, Rosangela\"},{\"Person.name\":\"Santos, Nuno C.\"}] |
| datacite.contributors.contributor.contributorName.fl_str_mv | Repositório Científico de Acesso Aberto da ULisboa |
| datacite.creators.creator.creatorName.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. |
| datacite.date.Accepted.fl_str_mv | 2013-01-01T00:00:00Z |
| datacite.date.available.fl_str_mv | 2014-03-06T11:25:01Z |
| datacite.date.embargoed.fl_str_mv | 2014-03-06T11:25:01Z |
| datacite.rights.fl_str_mv | http://purl.org/coar/access_right/c_16ec |
| datacite.subjects.subject.fl_str_mv | Lipopolysaccharide AMP rBPI21 Membrane binding Microcalorimetry SAXS |
| datacite.titles.title.fl_str_mv | rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures |
| dc.contributor.none.fl_str_mv | Repositório Científico de Acesso Aberto da ULisboa |
| dc.creator.none.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.date.Accepted.fl_str_mv | 2013-01-01T00:00:00Z |
| dc.date.available.fl_str_mv | 2014-03-06T11:25:01Z |
| dc.date.embargoed.fl_str_mv | 2014-03-06T11:25:01Z |
| dc.format.none.fl_str_mv | application/pdf |
| dc.identifier.none.fl_str_mv | http://dx.doi.org/10.1016/j.bbamem.2013.06.009 |
| dc.language.none.fl_str_mv | eng |
| dc.publisher.none.fl_str_mv | Elsevier |
| dc.rights.none.fl_str_mv | http://purl.org/coar/access_right/c_16ec |
| dc.subject.none.fl_str_mv | Lipopolysaccharide AMP rBPI21 Membrane binding Microcalorimetry SAXS |
| dc.title.fl_str_mv | rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures |
| dc.type.none.fl_str_mv | http://purl.org/coar/resource_type/c_6501 |
| description | rBPI21 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. |
| dirty | 0 |
| eu_rights_str_mv | restrictedAccess |
| format | article |
| fulltext.url.fl_str_mv | https://repositorio.ulisboa.pt/bitstreams/d81a56e2-dce6-498b-9904-cead5851f64c/download |
| id | ul_9ecaa33827be23c7a6ce59ef4e2bcdc2 |
| identifier.doi.fl_str_mv | http://dx.doi.org/10.1016/j.bbamem.2013.06.009 |
| instacron_str | ul |
| institution | Universidade de Lisboa |
| instname_str | Universidade de Lisboa |
| language | eng |
| network_acronym_str | ul |
| network_name_str | Repositório da Universidade de Lisboa |
| oai_identifier_str | oai:repositorio.ulisboa.pt:10451/10691 |
| organization_str_mv | urn:organizationAcronym:ul |
| person_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. |
| publishDate | 2013 |
| publisher.none.fl_str_mv | Elsevier |
| reponame_str | Repositório da Universidade de Lisboa |
| repository_id_str | urn:repositoryAcronym:ul |
| service_str_mv | urn:repositoryAcronym:ul |
| spelling | engElsevierengrBPI21 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.application/pdfengrBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structuresDomingues, Marco M.Bianconi, M. LuciaBarbosa, Leandro R. S.Santiago, Patrícia S.Tabak, MarcelCastanho, Miguel A. R. B.Itri, RosangelaSantos, Nuno C.HostingInstitutionOrganizationalRepositório Científico de Acesso Aberto da ULisboae-mailmailto:repositorio@reitoria.ulisboa.ptrepositorio@reitoria.ulisboa.ptHandlehttp://hdl.handle.net/10451/10691ISSNIsPartOf0006-30022014-03-06T11:25:01Z20132013-01-01T00:00:00ZDOIhttp://dx.doi.org/10.1016/j.bbamem.2013.06.009http://purl.org/coar/access_right/c_16ecrestricted accessLipopolysaccharideAMPrBPI21Membrane bindingMicrocalorimetrySAXS1531161 bytesliteraturehttp://purl.org/coar/resource_type/c_6501journal articlehttp://purl.org/coar/access_right/c_16ecapplication/pdffulltexthttps://repositorio.ulisboa.pt/bitstreams/d81a56e2-dce6-498b-9904-cead5851f64c/downloadBiochimica et Biophysica Acta182824192427 |
| spellingShingle | rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures Domingues, Marco M. Lipopolysaccharide AMP rBPI21 Membrane binding Microcalorimetry SAXS Domingues, Marco M. Lipopolysaccharide AMP rBPI21 Membrane binding Microcalorimetry SAXS |
| status | SINGLETON |
| subject.fl_str_mv | Lipopolysaccharide AMP rBPI21 Membrane binding Microcalorimetry SAXS |
| title | 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 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 rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures |
| title_short | 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 |
| topic | Lipopolysaccharide AMP rBPI21 Membrane binding Microcalorimetry SAXS |
| topic_facet | Lipopolysaccharide AMP rBPI21 Membrane binding Microcalorimetry SAXS |
| url | http://dx.doi.org/10.1016/j.bbamem.2013.06.009 |
| visible | 1 |