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1 2016

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Budowa i funkcje układów białkowo-lipidowych

Litwińczuk-Mammadova A., Cieślik-Boczula K., Rospenk M.

Wiadomości Chemiczne

2016

[Z] 70, 11-12

723--746

Biomembranes play many structural and functional roles in both prokaryotic and eukaryotic cells [10]. They define compartments, the communication between the inside and outside of the cell. The main components of biomembranes are lipids and proteins, which form protein-lipid bilayer systems [10]. A structure and physicochemical properties of protein-lipid membranes, which determines biological activities of biomembranes, are strongly dependent on interactions between lipid and protein components and external agents such as a temperature, pH, and a membrane hydration [4]. A lipid bilayer matrix serves as a perfect environment for membrane proteins (Fig. 1), and it assures activities of these proteins. Because biomembranes are composed of many different groups of lipids and proteins and have a complex structure, it is difficult to study in details their physicochemical properties using physicochemical methods. For these reason, lipid membranes of liposomes are used in many scientific laboratories for studding processes associated with a lipid phase transition, a membrane hydration, or protein-membrane interactions. The structure of liposomes (Fig. 5), and an influence of pH and an ionic strength on a lipid bilayer structure are discussed in the presented work. The role of membrane proteins in determination of biological activities of biomembranes is highlighted. A high variety of a structure and an enzymatic activity of membrane proteins is responsible for a high diversity of biological functions of cell membranes [2]. α-Lactalbumin (α-LA) is a peripheral membrane protein (Figs 8 and 9), its biological function is strongly related to its conformational structure and interaction with lipid membranes [49]. The complex of α-LA in a molten globule conformational state with oleic acid, termed as a HAMLET complex, are disused in a context of its anti-tumor activity.