Hemoglobin binding to phospholipid membranes as revealed by pyrene fluorescence study

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dc.contributor.authorKutsenko, O.K.
dc.contributor.authorGorbenko, G.P.
dc.contributor.authorTrusova, V.M.
dc.date.accessioned2012-12-04T00:39:34Z
dc.date.available2012-12-04T00:39:34Z
dc.date.issued2011
dc.description.abstractIn this work hemoglobin (Hb) association with lipid bilayers was investigated using fluorescent probe pyrene. Model membranes were prepared from zwitterionic lipid phosphatidylcholine (PC), anionic lipid phosphatidylglycerol (PG) and cholesterol (Chol). Hb-lipid binding was followed by the pyrene fluorescence quenching. Hb-induced decrease of pyrene monomer fluorescence was followed by the increase of relative intensities of vibronic bands. Presumably, Hb penetration into the bilayer increases the space between neighbouring lipids and promotes water penetration into the membrane core. Pyrene excimer emission quenching was interpreted in terms of resonance energy transfer. The greatest depth of Hb penetration into the lipid bilayer was observed in PC vesicles. In Chol-containing liposomes sterol condensing effect prevents deep protein penetration into the membrane. PG has an ability to stabilize lipid bilayers due to the ordered state of its lipid tails and H-bonding interactions between lipid molecules. This also can prevent Hb access to the inner membrane regions.en
dc.identifier.citationЖурналen
dc.identifier.urihttps://ekhnuir.karazin.ua/handle/123456789/7234
dc.language.isoenen
dc.publisherХарьковский Национальный Университет им. В.Н.Каразинаen
dc.relation.ispartofseriesБиофизический вестник;26(1)
dc.subjecthemoglobinen
dc.subjectmodel membranesen
dc.subjectprotein-lipid complexesen
dc.subjectpyreneen
dc.subjectfluorescence spectroscopyen
dc.titleHemoglobin binding to phospholipid membranes as revealed by pyrene fluorescence studyen
dc.typeArticleen

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