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dc.contributor.authorBaumann, Anne
dc.contributor.authorGjerde, Anja Underhaug
dc.contributor.authorYing, Ming
dc.contributor.authorSvanborg, Catharina
dc.contributor.authorHolmsen, Holm A
dc.contributor.authorGlomm, Wilhelm
dc.contributor.authorMartinez, Aurora
dc.contributor.authorHalskau jr, Øyvind
dc.date.accessioned2015-04-01T07:41:18Z
dc.date.accessioned2016-06-20T10:24:27Z
dc.date.available2015-04-01T07:41:18Z
dc.date.available2016-06-20T10:24:27Z
dc.date.issued2012
dc.identifier.citationJournal of Molecular Biology 2012, 418(1-2):90-102nb_NO
dc.identifier.issn0022-2836
dc.identifier.urihttp://hdl.handle.net/11250/2393192
dc.description.abstractRecently, the anticancer activity of human α-lactalbumin made lethal to tumor cells (HAMLET) has been linked to its increased membrane affinity in vitro, at neutral pH, and ability to cause leakage relative to the inactive native bovine α-lactalbumin (BLA) protein. In this study, atomic force microscopy resolved membrane distortions and annular oligomers (AOs) produced by HAMLET when deposited at neutral pH on mica together with a negatively charged lipid monolayer. BLA, BAMLET (HAMLET's bovine counterpart) and membrane-binding Peptide C, corresponding to BLA residues 75–100, also form AO-like structures under these conditions but at higher subphase concentrations than HAMLET. The N-terminal Peptide A, which binds to membranes at acidic but not at neutral pH, did not form AOs. This suggests a correlation between the capacity of the proteins/peptides to integrate into the membrane at neutral pH—as observed by liposome content leakage and circular dichroism experiments—and the formation of AOs, albeit at higher concentrations. Formation of AOs, which might be important to HAMLET's tumor toxic action, appears related to the increased tendency of the protein to populate intermediately folded states compared to the native protein, the formation of which is promoted by, but not uniquely dependent on, the oleic acid molecules associated with HAMLET.nb_NO
dc.language.isoengnb_NO
dc.publisherElseviernb_NO
dc.rightsNavngivelse-Ikkekommersiell-IngenBearbeidelse 3.0 Norge*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/no/*
dc.titleHAMLET forms annular oligomers when deposited with phoshpolipid monolayersnb_NO
dc.typeJournal articlenb_NO
dc.typePeer reviewednb_NO
dc.date.updated2015-04-01T07:41:18Z
dc.subject.nsiVDP::Medisinske fag: 700::Basale medisinske, odontologiske og veterinærmedisinske fag: 710::Medisinsk molekylærbiologi : 711nb_NO
dc.subject.nsiVDP::Midical sciences: 700::Basic medical, dental and veterinary sciences: 710::Medical molecular biology: 711nb_NO
dc.source.volume418nb_NO
dc.source.journalJournal of Molecular Biologynb_NO
dc.identifier.doi10.1016/j.jmb.2012.02.006
dc.identifier.cristin919486
dc.description.localcode© 2012 Elsevier Ltd. Open access under CC BY-NC-ND license.nb_NO


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