Budowa i funkcje układów białkowo-lipidowych

• Autorzy: Litwińczuk-Mammadova A. , Cieślik-Boczula K. , Rospenk M.

Warianty tytułu

EN

Structure and function of protein-lipid systems

• Języki publikacji: PL

Abstrakty

EN

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.

Słowa kluczowe

PL

odziaływania białko-lipid; liposomy DPPC; przejścia fazowe; α-laktoalbumina; kompleks HAMLET/BAMLET; stopiona globula

EN

lipid-protein interactions; DPPC liposomes; phase transitions; α-lactalbumin; complex HAMLET/BAMLET; molten globule state

• Wydawca: Polskie Towarzystwo Chemiczne
• Czasopismo: Wiadomości Chemiczne
• Rocznik: 2016
• Tom: [Z] 70, 11-12
• Strony: 723--746
• Opis fizyczny: Bibliogr. 64 poz., rys.

Twórcy

autor

Litwińczuk-Mammadova A.

• Uniwersytet Wrocławski, Wydział Chemii, ul. F. Joliot-Curie 14, 50-383 Wrocław

autor

Cieślik-Boczula K.

• Uniwersytet Wrocławski, Wydział Chemii, ul. F. Joliot-Curie 14, 50-383 Wrocław

autor

Rospenk M.

• Uniwersytet Wrocławski, Wydział Chemii, ul. F. Joliot-Curie 14, 50-383 Wrocław

Bibliografia

• [1] G. Karp, Cell and molecular biology: concepts and experiments, John Wiley, 2010.
• [2] S.J. Singel, G.L. Nicolson, Science, 1972, 175, 720.
• [3] K. Sugano, Artificial Membrane Technologies to Assess Transfer and Permeation of Drugs in Drug Discovery, [w:] John B. Taylor, David J. Triggle, Comprehensive Medicinal Chemistry, tom II, Elsevier, 2007.
• [4] M. Pasenkiewicz-Gierula, KOSMOS, 2009, 58, 49.
• [5] E.P. Solomon, L.R. Berg, D.W. Martin, Biology, Thomson Books/Cole, Belmont USA 2008.
• [6] B. Alberts, Podstawy biologii komórek 2, Wydawnictwo Naukowe PWN, Warszawa 2005.
• [7] K. Dołowy, A. Szewczyk, S. Pikuła, Błony biologiczne, Wydawnictwo „Śląsk”, Katowice – Warszawa 2003.
• [8] J. Ulander, A.D.J. Haymet, Biophys. J., 2003, 85, 3475.
• [9] A. Kozubek, A.F. Sikorski, J. Szopa, Molekularna organizacja komórek, tom II, Lipidy, liposomy i błony biologiczne, Wydawnictwo Uniwersytetu Wrocławskiego, Wrocław 1996.
• [10] L. Stryer, Biochemia, Wydawnictwo Naukowe PWN, Warszawa 2003.
• [11] G. Tresset, PMC Biophysics, 2009, 2, 1.
• [12] C. Chipot, M.L. Klein, M. Tarek, Modeling lipid membranes, [w:] Handbook of Materials Modeling, S. Yip (red.), Springer, Netherlands 2005.
• [13] D.E. Vance, J.E. Vance, Biochemistry of Lipids, Lipoproteins and Membranes, Elsevier, 2008.
• [14] R. Koynova, M. Caffrey, Biochim. Biophys. Acta, 1998, 1376, 91.
• [15] B. Alberts, A. Johnson, J. Lewis, Molecular Biology of the Cell, Garland Science, New York 2002.
• [16] A. Laouini, C. Jaafar-Maalej, I. Limayem-Blouza, S. Sfar, C. Charcosset, H. Fessi, J. Colloid Sci. Biotechnol, 2012, 1, 147.
• [17] Y. P. Patil, S. Jadhav, Chem. Phys. Lipids, 2014, 177, 18.
• [18] D. Bitounis, R. Fanciullino, A.Iliadis, J. Ciccolini, ISRN Pharm., 2012, 2012, 1.
• [19] V.V. Mody, M.I. Nounou, M. Bikram, Adv. Drug Deliv. Rev., 2009, 61, 795.
• [20] A.D. Bangham, Adv. Lipid Res., 1963, 1, 63.
• [21] G. Sessa, G. Weissmann, J. Lipid Res., 1968, 9, 310.
• [22] D. Chapman, Q. Rev. Biophys., 1975, 8, 185.
• [23] A. Tardieu, V. Luzzati, F. C. Reman, J. Mol. Biol., 1973, 75, 711.
• [24] T. Le Bihan, M. Pezolet, Chem. Phys. Lipids, 1998, 94, 13.
• [25] R.N.A.H. Lewis, R.N. McElhaney, The Mesomorphic Phase Behavior of Lipid Bilayers, [w:] The Structure of Biological Membranes, P. L. Yeagle (red), CRC Press, 2005.
• [26] D. Marsh, Chem. Phys. Lipids, 2012, 165, 59.
• [27] S. Tristram-Nagle, R. Zhang, R.M. Suter, C.R. Worthington, W.J. Sun, J.F. Nagle,Biophys. J., 1993, 64, 1097.
• [28] D.M. Small, R.A. Zoeller, Lipids, Structure and Biochemistry of, [w:] Encyclopedia of Human Biology, Tom 4, Academic Press, Inc., 1991, 725.
• [29] M. Kranenburg, B. Smit, J. Phys. Chem. B, 2005, 109, 6553.
• [30] J.M. Rodgers, J. Sorensen, F.J.-M. de Meyer , B. Schiott, B. Smit, J. Phys. Chem. B, 2012, 116, 1551.
• [31] M. Eeman, M. Deleu, Biotechnol. Agron. Soc. Environ., 2010, 14, 719.
• [32] T. Kaasgaard, C.J. Drummond, Phys. Chem. Chem. Phys., 2006, 8, 4957.
• [33] J. Yin, Y.-P. Zhao, J. Colloid Interface Sci., 2009, 329, 410.
• [34] U. Essmann, L. Perera, M.L. Berkowitz, Langmuir, 1995, 11, 4519.
• [35] M. Pasenkiewicz-Gierula, Y. Takaoka, H. Miyagawa, K. Kitamura, A. Kusumi, J. Phys. Chem. A, 1997, 101, 3677.
• [36] H. Trauble, M. Teubner, P. Woolley, H. Eibl, Biophys. Chem., 1976, 4, 319.
• [37] M. Langner, K. Kubica, Chem. Phys. Lipids, 1999, 101, 3.
• [38] A. Lucero, M.R. Rodriguez Nino, A.P. Gunning, V.J. Morris, P.J. Wilde, J.M. Rodriguez Patino, J. Phys. Chem. B, 2008, 112, 7651.
• [39] A. Lucero Caro, A.R. Mackie, A.P. Gunning, P.J. Wilde, V.J. Morris, M.R. Rodriguez Niño, J.M. Rodriguez Patino, Role of Electrostatic Interactions on Molecular Self-Assembly of Protein + Phospholipid Films at the Air–Water Interface, [w:] Food Colloids: Self-assembly and Material Science, E. Dickinson, M.E. Leser (Red.), Royal Society of Chemistry, Cambridge 2007.
• [40] S. Furuike, V.G. Levadny, S.J. Li, M. Yamazaki, Biophys. J., 1999, 77, 2015.
• [41] R. Zimmermann, D. Kuttner, L. Renner, M. Kaufmann, J. Zitzmann, M. Muller, Biointerphases, 2009, 4, 1.
• [42] N.N. Casillas-Ituarte, X. Chen, H. Castada, H.C. Allen, J. Phys. Chem. B, 2010, 114, 9485
• [43] Z.K. Issa, Ch.W. Manke, B.P. Jena, J.J. Potoff, J. Phys. Chem. B, 2010, 114, 13249.
• [44] M.G. Ganesan, D.L. Schwinke, N. Weiner, Biochim. Biophys. Acta Biomembranes, 1982, 686, 245.
• [45] R.A. Bockmann, A. Hac, T. Heimburg, H. Grubmuller, Biophys. J., 2003, 85, 1647.
• [46] A.A. Gurtovenko, J. Chem. Phys., 2005, 122, 244902.
• [47] D.M. Engelman, T.A. Steitz, A. Goldman, Ann. Rev. Biophys. Biophys. Chem., 1986, 15, 321.
• [48] A.V. Agasoster, O. Halskau, E. Fuglebakk, N.A. Froystein, A. Muga, H. Holmsen, A. Martinez, J. Biol. Chem., 2003, 278, 21790.
• [49] E.A. Permyakov, αLactalbumin, Nova Science Publishers, Inc., Nowy York 2005.
• [50] N.J. Kuhn, D.T. Carrick, C.J. Wilde, J. Dairy Sci., 1980, 63, 328.
• [51] K. Brew, F.J. Castellino, T.C. Vanaman, R.L. Hill, J. Biol. Chem., 1970, 245, 4570.
• [52] E.D. Chrysina, K. Brew, K.R. Acharya, J. Biol. Chem., 2000, 275, 37021.
• [53] K. Kuwajima, FASEB J., 1996, 10, 102.
• [54] R. Wijesinha-Bettoni, C.M. Dobson, C. Redfield, J. Mol. Biol., 2001, 312, 261.
• [55] O.B. Ptitsyn, Biochemistry, 1997, 63, 367.
• [56] O.B. Ptitsyn, V.N. Uversky, FEBS Lett., 1994, 341, 15.
• [57] K.H. Mok, J. Pettersson, S. Orrenius, C. Svanborg, Biochem. Biophys. Res. Comm., 2007, 354, 1.
• [58] L. Gustafsson, O. Hallgren, A.-K. Mossberg, J. Pettersson, W. Fischer, A. Aronsson, C. Svanborg, J. Nut., 2005, 135, 1299.
• [59] M. Svensson, A. Hakansson, A.-K. Mossberg, S. Linse, and C. Svanborg, PNAS, 2000, 97, 4221.
• [60] J. Krol, A. Litwińczuk, A. Zarajczyk, Z. Litwińczuk, Medycyna Wet., 2008, 64, 1375.
• [61] I. Hanssens, C. Houthuys, W. Herreman, F.H. van Cauwelaert, Biochim. Biophys. Acta, 1980, 602, 539.
• [62] W. Herreman, P. van Tornout, F.H. van Cauwelaert, I. Hanssens, Biochim. Biophys. Acta, 1981, 640, 419.
• [63] I. Hanssens, J.C. van Ceunebroeck, H. Pottel, G. Preaux, F. van Cauwelaert, Biochim. Biophys. Acta, 1985, 817, 154.
• [64] J.P. Segrest, Chem. Phys. Lipids, 1977, 18, 7.

Uwagi

Opracowanie ze środków MNiSW w ramach umowy 812/P-DUN/2016 na działalność upowszechniającą naukę (zadania 2017).