Počet záznamů: 1  

Bilayer Localization of Membrane-Active Peptides Studied in Biomimetic Vesicles by Visible and Fluorescence Spectroscopies

  1. 1.
    0181772 - UFCH-W 20030211 RIV DE eng J - Článek v odborném periodiku
    Sheynis, T. - Sýkora, Jan - Benda, Aleš - Kolusheva, S. - Hof, Martin - Jelinek, R.
    Bilayer Localization of Membrane-Active Peptides Studied in Biomimetic Vesicles by Visible and Fluorescence Spectroscopies.
    European Journal of Biochemistry. Roč. 270, č. 22 (2003), s. 4478-4487. ISSN 0014-2956
    Grant CEP: GA MŠk LN00A032
    Výzkumný záměr: CEZ:AV0Z4040901
    Klíčová slova: solvent relaxation * fluorescence correlation spectroscopy * lipid bilayers
    Kód oboru RIV: CF - Fyzikální chemie a teoretická chemie
    Impakt faktor: 3.001, rok: 2003

    Depth of bilayer penetration and effects on lipid mobility conferred by the membrane-active peptides magainin, melittin, and a hydrophobic helical sequence KKA(LA)(7)KK (denoted KAL), were investigated by colorimetric and time-resolved fluorescence techniques in biomimetic phospholipid/poly(diacetylene) vesicles. The experiments demonstrated that the extent of bilayer permeation and peptide localization within the membrane was dependent upon the bilayer composition, and that distinct dynamic modifications were induced each peptide within the head-group environment of the phospholipids. Solvent relaxation, fluorescence correlation spectroscopy and fluorescence quenching analyses, employing probes at different locations within the bilayer, showed that magainin and melittin inserted close to the glycerol residues in bilayers incorporating negatively charged phospholipids, but predominant association at the lipid-water interface occurred in bilayers containing zwitterionic phospholipids.
    Trvalý link: http://hdl.handle.net/11104/0078293