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The study of interaction between surface viral proteins and model phospholipids is important for learning more  details about the mechanisms of viral penetration into cells during infection. In this context, liposomes represent  suitable systems for modeling a cell membrane. The binding of hemagglutinin (HA) of influenza virus with  phosphatidylcholine liposomes was studied by equilibrium adsorption. It was interesting elucidate changes occurring  in the structure of a protein during its translocation from the surface into the interior part of the membrane. In this work,  we have studied characteristics of the protein-lipid interaction during HA complex formation with phospholipids  including adsorption of HA on a phospholipid bilayer. Using the Scatchard equation and the Gibbs-Helmholtz equation  at pH 4.0 and pH 6.0 thermodynamic parameters were determined. The results concluded the hydrophobic type  of interaction between viral protein and liposomes. The additional confirmation of hydrophobic protein-lipid interaction  presence was determination of HA distribution constants in two-phase systems: dextran-polyethylene glycol (K1) and  dextran-polyethylene glycol esterified with palmitic acid (K2). The presence of hydrophobic interaction between HA  and the liposome membrane was also confirmed using the quenching method of intrinsic protein fluorescence  by a neutral quencher with acrylamide. At pH 4.0, an increase in the Stern-Volmer quenching constant was observed  for the HA+liposome from phosphatidylcholine system, which is caused by structural changes in HA upon  incorporation into the liposome bilayer. The fluorescence quenching rate constants calculated using the Stern-Volmer  equation indicate a static quenching mechanism in which the quencher interacts with fluophors of a stationary protein  molecule. The obtained results are interesting for not only studying virus and cell fusion theoretically, but also have  practical applications. Using values of the protein-bilayer binding constant and free energy constant, it is possible  to select the optimal phospholipid composition of liposomes or virosomes to obtain a stronger complex with various  viral proteins. With two-phase systems, it is possible to determine the presence of hydrophobic sites on the viral protein  surface, which can be used for evaluation both protein-lipid and protein-protein interaction.

biomedicinskaâ himiâ

Determination of thermodynamic binding parameters and type of interaction between the А/Bangkok/1/1979 (Н3N2) influenza virus hemagglutinin and phosphatidylcholine liposome