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dc.contributor.author | Torrent-Sucarrat, Miquel | - |
dc.contributor.author | Cuyàs, Elisabet | - |
dc.contributor.author | Carreras-Colom, Ester | - |
dc.contributor.author | Navarro, Susanna | - |
dc.contributor.author | López Serrano, Olga | - |
dc.contributor.author | Maza, Alfons de la | - |
dc.contributor.author | Nogués, M. Victòria | - |
dc.contributor.author | Reshetnyak, Yana K. | - |
dc.contributor.author | Boix, Ester | - |
dc.date.accessioned | 2009-01-19T11:08:06Z | - |
dc.date.available | 2009-01-19T11:08:06Z | - |
dc.date.issued | 2007-01-23 | - |
dc.identifier.citation | Biochemistry 46(3): 720-733 (2007) | en_US |
dc.identifier.issn | 1520-4995 | - |
dc.identifier.uri | http://hdl.handle.net/10261/9694 | - |
dc.description | 14 pages, 6 figures.-- PMID: 17223693 [PubMed].-- Available online on Dec 29, 2006. | en_US |
dc.description.abstract | The eosinophil cationic protein (ECP) is an antipathogen protein involved in the host defense system. ECP displays bactericidal and membrane lytic capacities [Carreras et al. (2003) Biochemistry 42, 6636-6644]. We have now characterized in detail the protein-membrane interaction process. All observed fluorescent parameters of the wild type and single-tryptophan-containing mutants, as well as the results of decomposition analysis of protein fluorescence, suggest that W10 and W35 belong to two distinct spectral classes I and III, respectively. Tryptophan residues were classified and assigned to distinct structural classes using statistical approaches based on the analysis of tryptophan microenvironment structural properties. W10 belongs to class I and is buried in a relative nonpolar, nonflexible protein environment, while W35 (class III) is fully exposed to free water molecules. Tryptophan solvent exposure and the depth of the protein insertion in the lipid bilayer were monitored by the degree of protein fluorescence quenching by KI and brominated phospholipids, respectively. Results indicate that W35 partially inserts into the lipid bilayer, whereas W10 does not. Further analysis by electron microscopy and dynamic light scattering indicates that ECP can destabilize and trigger lipid vesicle aggregation at a nanomolar concentration range, corresponding to about 1:1000 protein/lipid ratio. No significant leakage of the vesicle aqueous content takes place below that protein concentration threshold. The data are consistent with a membrane destabilization “carpet-like” mechanism. | en_US |
dc.description.sponsorship | This work was supported by the Ministerio de Educación y Cultura (Grant BMC2003-08485-C02-01) and by the "Fundació La Marató de TV3" (TV3-031110). M.T. and E.C. are the recipients of predoctoral fellowships from the Generalitat de Catalunya, and S.N. is the recipient of a predoctoral fellowship from the Ministerio de Ciencia y Tecnología, Spain. | en_US |
dc.format.extent | 19968 bytes | - |
dc.format.mimetype | application/msword | - |
dc.language.iso | eng | en_US |
dc.publisher | American Chemical Society | en_US |
dc.rights | closedAccess | en_US |
dc.subject | Membrane | en_US |
dc.subject | Interaction mechanism | en_US |
dc.subject | Eosinophil Cationic Protein (ECP) | en_US |
dc.subject | Membrane destabilization | en_US |
dc.title | Topography studies on the membrane interaction mechanism of the eosinophil cationic protein | en_US |
dc.type | artículo | en_US |
dc.identifier.doi | 10.1021/bi061190e | - |
dc.description.peerreviewed | Peer reviewed | en_US |
dc.relation.publisherversion | http://dx.doi.org/10.1021/bi061190e | en_US |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairetype | artículo | - |
item.grantfulltext | none | - |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | No Fulltext | - |
item.languageiso639-1 | en | - |
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