Characteristics of binding of zwitterionic liposomes to water-soluble proteins
- 49 Downloads
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).
Key wordsphosphatidylcholine phosphatidylethanolamine liposomes aprotinin Bowman-Birk soybean proteinase inhibitor differential scanning calorimetry
Bowman-Birk soybean proteinase inhibitor
Unable to display preview. Download preview PDF.
- 2.Martynova, O. M., Tiourina, O. P., Selischeva, A. A., Sorokoumova, G. M., Shvets, V. I., and Larionova, N. I. (2000) Biochemistry (Moscow), 65, 1049–1054.Google Scholar
- 10.Sorokoumova, G. M., Selischeva, A. A., and Kaplun, A. P. (2000) Phospholipids. Methods of Isolation and Detection. Study of Physicochemical Properties of Lipid Dispersions in Water. Manual for Bioorganic Chemistry [in Russian], MITKhT Publishers, Moscow.Google Scholar
- 11.Bakina, A. S., Selischeva, A. A., and Larionova, N. I. (2008) Biomed. Khim., 54, 441–449.Google Scholar
- 15.Rance, M., and Byrd, R. A. (1983) J. Magn. Res., 52, 221–240.Google Scholar
- 16.Balkina, A. S., Selischeva, A. A., Sorokoumova, G. M., Ollivon, M., and Larionova, N. I. (2006) J. Drug Deliv. Sci. Tech., 16, 301–306.Google Scholar
- 20.Gennis, R. (1997) Biomembranes: Molecular Structure and Function [Russian translation] Mir, Moscow.Google Scholar
- 23.Lakowicz, J. R. (1999) Principles of Fluorescence Microscopy, 2nd Edn., Plenum Press, N. Y.Google Scholar
- 26.Gutbert, T., Frank, J., Bradaczek, H., and Fischer, W. (1997) J. Bacteriol., 79, 2879–2883.Google Scholar
- 32.Bach, D. (1983) in Biomembrane Structure and Function (Chapman, D., ed.) MacMillan Press, London, pp. 1–41.Google Scholar
- 35.Jung, J. E., and Kim, H. (1990) J. Biochem. (Tokyo), 107, 530–534.Google Scholar