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dc.contributor.authorTorrent-Sucarrat, Miquel-
dc.contributor.authorCuyás, Elisabet-
dc.contributor.authorCarreras-Colom, Ester-
dc.contributor.authorNavarro, Susanna-
dc.contributor.authorLópez Serrano, Olga-
dc.contributor.authorMaza, Alfons de la-
dc.contributor.authorNogués, M. Victòria-
dc.contributor.authorReshetnyak, Yana K.-
dc.contributor.authorBoix, Ester-
dc.date.accessioned2009-01-19T11:08:06Z-
dc.date.available2009-01-19T11:08:06Z-
dc.date.issued2007-01-23-
dc.identifier.citationBiochemistry 46(3): 720-733 (2007)en_US
dc.identifier.issn1520-4995-
dc.identifier.urihttp://hdl.handle.net/10261/9694-
dc.description14 pages, 6 figures.-- PMID: 17223693 [PubMed].-- Available online on Dec 29, 2006.en_US
dc.description.abstractThe 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.sponsorshipThis 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.extent19968 bytes-
dc.format.mimetypeapplication/msword-
dc.language.isoengen_US
dc.publisherAmerican Chemical Societyen_US
dc.rightsclosedAccessen_US
dc.subjectMembraneen_US
dc.subjectInteraction mechanismen_US
dc.subjectEosinophil Cationic Protein (ECP)en_US
dc.subjectMembrane destabilizationen_US
dc.titleTopography studies on the membrane interaction mechanism of the eosinophil cationic proteinen_US
dc.typeartículoen_US
dc.identifier.doihttp://dx.doi.org/10.1021/bi061190e-
dc.description.peerreviewedPeer revieweden_US
dc.relation.publisherversionhttp://dx.doi.org/10.1021/bi061190een_US
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