Characteristics of binding of zwitterionic liposomes to water-soluble proteins |
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Authors: | A S Dudkina A A Selischeva N I Larionova |
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Institution: | 1.Chemical Faculty,Lomonosov Moscow State University,Moscow,Russia;2.Biological Faculty,Lomonosov Moscow State University,Moscow,Russia |
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Abstract: | The interactions of zwitterionic phospholipids phosphatidylcholine and phosphatidylethanolamine with protein proteinase inhibitors
aprotinin and Bowman-Birk soybean proteinase inhibitor have been investigated. An increase in the hydrophobicity of the liposome
surface was shown to be an important factor for the formation of proteoliposomes. According to 31P-NMR spectra, incorporation of the proteins into the liposomes does not influence the structural organization of the surface
of the liposomes. Increasing the ionic strength does not inhibit the process of proteoliposome formation. Fluorescence assay
of the complexes of anthracene-labeled phospholipids with the rhodamine B-labeled protein showed that after the encapsulation
into the liposomes, the protein is located inside the particles and between the bilayers. Also, the effect of phospholipids
with saturated fatty acid residues on the protein-lipid interaction was studied by differential scanning calorimetry. The
results indicate that water-soluble proteins efficiently interact with zwitterionic phospholipids, and the encapsulation of
the proteins into the liposomes is provided by electrostatic and hydrophobic forces (in the case of aprotinin) or predominantly
by hydrophobic forces (Bowman-Birk soybean proteinase inhibitor). |
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Keywords: | |
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