Interactions between various milk proteins and small unilamellar liposomes at \(\mathrm{pH} 6.2\) have been followed by measuring the increase in the hydrodynamic radius of the particles using photon correlation spectroscopy. Relatively high salt concentration was required for adsorption of the prot
Size Dependence of Protein-Induced Flocculation of Phosphatidylcholine Liposomes
β Scribed by Mariana N. Dimitrova; Roumen Tsekov; Hideo Matsumura; Kunio Furusawa
- Publisher
- Elsevier Science
- Year
- 2000
- Tongue
- English
- Weight
- 883 KB
- Volume
- 226
- Category
- Article
- ISSN
- 0021-9797
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β¦ Synopsis
The adsorption of lysozyme and cytochrome C on phosphatidylcholine liposomes essentially changes the physical properties of the phospholipid membranes and under certain circumstances greatly affects the stability of the colloid dispersion by inducing bridging liposome flocculation. This study was designed to examine experimentally the influence of liposome size on two kinetic parameters of the flocculation, its rate constant and activation energy. As the liposome radius increased in the range 50-500 nm, the activation energy tended to decrease, resulting in an increased flocculation rate, except for the flocculation of 400-nm liposomes, which was greatly impeded. The pronounced influence of the liposome size on the flocculation rate constant was evident, since a well-defined minimum in the kinetic rate of flocculation of 400-nm liposomes was detected experimentally. The obtained nonlinear radius dependencies of the flocculation rates and activation energies are interpreted in terms of the bridging mechanism of the protein-induced liposome flocculation and the supplementary concept of the stability of thin liquid films formed between approaching protein-adsorbed liposomes.
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The Ca2Γ·-dependent interaction of various polyanionic polysaccharides (chondroitin sulfate, heparin, dextran sulfate,/~-cyclodextrin sulfate, hyaluronic acid and carboxymethyldextran) with multilamellar dimyristoyl phosphatidylcholine (DMPC) liposomes was investigated by calorimetric and fluorescenc
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