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 MŠMT 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