Hemoglobin binding to phospholipid membranes as revealed by pyrene fluorescence study

  • O. K. Kutsenko V.N. Karazin Kharkov National University
  • G. P. Gorbenko V.N. Karazin Kharkov National University
  • V. M. Trusova V.N. Karazin Kharkov National University
Keywords: hemoglobin, model membranes, protein-lipid complexes, pyrene, fluorescence spectroscopy

Abstract

In 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.

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Author Biographies

O. K. Kutsenko, V.N. Karazin Kharkov National University

4 Svobody Sq., Kharkov, 61022

G. P. Gorbenko, V.N. Karazin Kharkov National University

4 Svobody Sq., Kharkov, 61022

V. M. Trusova, V.N. Karazin Kharkov National University

4 Svobody Sq., Kharkov, 61022

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Cited
How to Cite
Kutsenko, O. K., Gorbenko, G. P., & Trusova, V. M. (1). Hemoglobin binding to phospholipid membranes as revealed by pyrene fluorescence study. Biophysical Bulletin, 1(26). Retrieved from https://periodicals.karazin.ua/biophysvisnyk/article/view/2710

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