Моделювання адсорбції білків на поверхню ліпідного моношару
Ключові слова:
ліпідний моношар, сорбція білків, ізотерма Фрумкіна
Анотація
З використанням модифікованого підходу Фрумкіна, проведено моделювання адсорбції білків на
поверхню ліпідного моношару з урахуванням різних типів білок-ліпідних взаємодій. Отримані
результати представлені у вигляді залежності зростання поверхневого тиску моношару при сорбції
білків ( ) від початкового поверхневого тиску ( 0). Теоретичні криві були розраховані при
варіюванні ряду параметрів взаємодій. Зроблено припущення, що поведінка залежностей 0 ( )
дозволяє розрізнити між поверхневою локалізацією білка та його вбудовуванням у ліпідний
моношар. Теоретичні розрахунки добре узгоджуються з експериментальними даними, наведеними
у літературі.
Завантаження
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Посилання
1. Porath J. Salting-out adsorption techniques for protein purification / J. Porath // Biopolymers. – 2004. – V. 26. – P. 193–204.
2. Adsorption of bovine serum albumin and lysozyme on siliceous MCM-41 / A. Katiyar, L. Ji, P. G. Smirniotis, N. G. Pinto // Micropor. Mesopor. Mater. – 2005. – V. 80. – P. 311–320.
3. Comparison of the protein adsorption selectivity of salt-promoted agarose-based adsorbents – hydrophobic, thiophilic and electron donor-acceptor adsorbents / P. P. Berna, N. Berna, J. Porath, S. Oscarsson // J. Chromat. A. – 1998. – V. 800. – P. 151–159.
4. Horbett T. A. Principles underlying the role of adsorbed plasma proteins in blood interactions with foreign materials / T. A. Horbett // Cardiovasc. Pathol. – 1993. – V. 2. – P. 137–148.
5. Characterization of self-assembled monolayers for biosensor applications / R. M. Nyquist, A. S. Eberhardt, L. A. Silks [et al.] // Langmuir. – 2000. – V. 16. – P. 1793–1800.
6. Selective protein adsorption and blood compatibility of hydroxycarbonate apatites / S. Takemoto, Y. Kusudo, K. Tsuru [et al.] // J. Biomed. Mater. Res. A. – 2004. – V. 69. – P. 544–551.
7. Bajpai A.K. Blood protein adsorption onto a polymeric biomaterial of polyethylene glycol and poly[(2-hydroxyethyl methacrylate)-co-acrylonitrile] and evaluation of in vitro blood compatibility / A. K. Bajpai // Polymer Internat. – 2005. – V. 54. – P. 304–315.
8. Tang L. Inflammatory responses to implanted polymeric biomaterials: role of surface-adsorbed immunoglobulin G / L. Tang, A. H. Lucas, J. W. Eaton // J. Lab. Clin. Med. – 1993. – V. 122. – P. 292–300.
9. Tang L. Fibrinogen adsorption and host tissue responses to plasma functionalized surfaces / L. Tang, Y. Wu, R. B. Timmons // J. Biomed. Mater. Res. – 1998. – V. 42. – P. 156–163.
10. Heimburg T. Themodynamics of the interaction of proteins with lipid membranes, In Biological Membranes: A molecular perspective from computation and experiment / T. Heimburg, D. Marsh // Birkhauser Boston. – 1996. – P. 405–462.
11. Sankaram M. Protein-lipid interactions with peripheral membrane proteins / M. Sankaram, D. Marsh // In Protein-Lipid Interactions, Elsevier. – 1993. P. 127–162.
12. Bray D. Signaling complexes: biophysical constraints on intracellular communication / D. Bray // Ann. Rev. Biophys. Biomol. Struct. – 1998. – V. 27. – P. 59–75.
13. Protein-induced fusion can be modulated by target membrane lipids through a structural switch at the level of the fusion peptide / E. I. Pecheur, I. Martin, A. Bienvenue [et al.] // J. Biol. Chem. – 2000. – V. 275. – P. 3936–3942.
14. A new model to describe extrinsic protein binding to phospholipid membranes of varying composition: application to human coagulation proteins / G. A. Cutsforth, R. N. Whitaker, J. Hermans, B. R. Lentz // Biochemistry. – 1989. – V. 28. – P. 7453–7461.
15. Cholera toxin assault on lipid monolayers containing ganglioside GM1 / C. E. Miller, J. Majewski, R. Faller [et al.] // Biophys. J. – 2004. – V. 86. – P. 3700–3708.
16. Protein adsorption on supported phospholipid bilayers / K. Glasmӓstar, C. Larsson, F. Höök, B. Kasemo // Colloid Interface Sci. – 2002. – V. 246. – P. 40–47.
17. Gorbenko G. P. Binding of lysozyme to phospholipid bilayers: evidence for protein aggregation upon membrane association / G. P. Gorbenko, V. M. Ioffe, P. K. J. Kinnunen // Biophys. J. – 2007. – V. 93. – P. 140–153.
18. Salafsky J. S. Protein adsorption at interfaces detected by second harmonic generation / J. S. Salafsky, K. B. Eisenthal // J. Phys. Chem. B. – 2000. – V. 104. – P. 7752–7755.
19. Morphological changes of supported lipid bilayers induced by lysozyme: planar domain formation vs. multilayer stacking / V.M. Trusova, G.P. Gorbenko, I. Akopova [et al.] // Colloids Surf. B. – 2010. – V. 80. – P. 219–226.
20. Dynamics of β-lactoglobulin penetration into Langmuir monolayers of 2D condensating phospholipid / V. B. Fainerman, J. Zhao, D. Vollhardt [et al.] // J. Phys. Chem. B. – 1999. – V. 103. – P. 8998–9007.
21. Peng J. B. The structure of Langmuir-Blodgett films of fatty acids and their salts / J. B. Peng, G. T Barnes, I. R. Gentle // Adv. Colloid Interface Sci. – 2001. – V. 91. – P. 163–219.
22. Brockman H. Lipid monolayers: why use half a membrane to characterize protein-membrane interactions / H. Brockman // Curr. Opin. Struct. Biol. – 1999. – V. 9. – P. 438–443.
23. Study of gramicidin A – phospholipid interactions in Langmuir monolayers: analysis of their mechanical, thermodynamical, and electrical properties / M. Weis, M. Vanco, P. Vitovic [et al.] // J. Phys. Chem. B. – 2006. – V. 110. – P. 26272–26278.
24. Interaction of myelin basic protein with phospholipid monolayers: mechanism of protein penetration / E. Polverini, S. Arisi, P. Cavatorta [et al.] // Langmuir. – 2003. – V. 19. – P. 872–877.
25. Molecular organization in protein-lipid film on the water surface studied by x-ray standing wave measurements under total external reflection / S. Zheludeva, N. Novikova, N. Stepina [et al.] // Spectrochim. Acta B. – 2008. – V. 63. – P. 1399–1403.
26. Pethica B. A. The thermodynamics of monolayer penetration at constant area. Part 1 / B. A. Pethica // Trans. Faraday Soc. – 1955. – V. 51. – P. 1402–1411.
27. Anderson P. J. The thermodynamics of monolayer penetration at constant area. Part 1 / P. J. Anderson, B. A. Pethica // Trans. Faraday Soc. – 1956. – V. 52. – P. 1080–1087.
28. Alexander D. M. Use of the Gibbs equation to calculate adsorption into monolayer-covered surfaces / D. M. Alexander, G. T. Barnes // J. Chem. Soc. Faraday Trans. 1. – 1980. – V. 76. – P. 118–125.
29. Thermodynamics of multicomponent monolayers: IV. Monolayer penetration / K. Motomura, Y. Hayami, M. Aratono, R. Matuura // J. Colloid Interface Sci. – P. 333–338.
30. Ter-Minassian-Saraga L. Penetration into insoluble monolayers. 1. A semiopen system behavior / L. Ter-Minassian-Saraga // Langmuir. – 1985. – V. 1. – P. 391–394.
31. Fainerman V. B. Penetration of Langmuir monolayers by soluble amphiphilic molecules / V. B. Fainerman, D. Vollhardt // Langmuir. – 1999. – V. 15. – P. 1784–1790.
32. Sundaram S. Equations for the equilibrium surface pressure increase on the penetration of an insoluble monolayer by soluble surfactant / S. Sundaram, K. J. Stebe // Langmuir. – 1996. – V. 12. – P. 2028–2034.
33. Datwani S. S. Monolayer penetration by a charged amphiphile: equilibrium and dynamics / S. S. Datwani, K. J. Stebe // Colloids Surf. A. – 2001. – V. 192. – P. 109–129.
34. Analysis of the contribution of saturated and polyunsaturated phospholipid monolayers to the binding of proteins / P. Calvez, É. Demers, E. Boisselier, C. Salesse // Langmuir. – 2011. – V. 27. – P. 1373–1379.
35. Influence of the physical state of phospholipid monolayers on protein binding / E. Boisselier, P. Calvez, É. Demers [et al.] // Langmuir. – 2012. – V. 28. – P. 9680–9688.
36. Benga G. Interactions between components in biological membranes and their implication for membrane function / G. Benga, R. Holmes // Progr. Biophys. Mol. Biol. – 1984. – V. 43. – P. 195–257.
37. Jahnig F. Thermodynamics and kinetics of protein incorporation into membranes / F. Jahnig // Proc. Natl. Acad. Sci. USA. – 1983. – V. 80. – P. 3691–3695.
38. Zuckermann M. J. Insertion and pore formation driven by adsorption of protein onto lipid bilayer membrane-water interface / M. J. Zuckermann, T. Heimburg // Biophys. J. – 2001. – V. 81. – P. 2458–2472.
39. Interaction of influenza virus hemagglutinin with a lipid monolayer. A comparison of the surface activities of intact virions, isolated hemagglutinins, and a synthetic fusion peptide / K. N. J. Burger, S. A. Wharton, R. A. Deme1, A. J. Verkleij // Biochemistry. – 1991. – V. 30. – P. 11173–11180.
40. Streptomyces chromofuscus phospholipase D interaction with lipidic activators at the air-water interface / K. E. Kirat, J. P. Chauvet, B. Roux, F. Besson // Biochim. Biophys. Acta. – 2004. – V. 1661. – P. 144–153.
41. Interactions of adriamycin, cytochrome c, and serum albumin with lipid monolayers containing poly(ethylene glycol)-ceramide / H. Zhao, P. M. Dubielecka, T. Soderlund, P. K. J. Kinnunen // Biophys. J. – 2002. – V. 83. – P. 954–967.
42. Thakur G. Surface chemistry of Alzheimer’s disease: a Langmuir monolayer approach / G. Thakur, M. Micic, R. M. Leblanc // Colloids Surf. B. – 2009. – V. 74. – P. 436–456.
2. Adsorption of bovine serum albumin and lysozyme on siliceous MCM-41 / A. Katiyar, L. Ji, P. G. Smirniotis, N. G. Pinto // Micropor. Mesopor. Mater. – 2005. – V. 80. – P. 311–320.
3. Comparison of the protein adsorption selectivity of salt-promoted agarose-based adsorbents – hydrophobic, thiophilic and electron donor-acceptor adsorbents / P. P. Berna, N. Berna, J. Porath, S. Oscarsson // J. Chromat. A. – 1998. – V. 800. – P. 151–159.
4. Horbett T. A. Principles underlying the role of adsorbed plasma proteins in blood interactions with foreign materials / T. A. Horbett // Cardiovasc. Pathol. – 1993. – V. 2. – P. 137–148.
5. Characterization of self-assembled monolayers for biosensor applications / R. M. Nyquist, A. S. Eberhardt, L. A. Silks [et al.] // Langmuir. – 2000. – V. 16. – P. 1793–1800.
6. Selective protein adsorption and blood compatibility of hydroxycarbonate apatites / S. Takemoto, Y. Kusudo, K. Tsuru [et al.] // J. Biomed. Mater. Res. A. – 2004. – V. 69. – P. 544–551.
7. Bajpai A.K. Blood protein adsorption onto a polymeric biomaterial of polyethylene glycol and poly[(2-hydroxyethyl methacrylate)-co-acrylonitrile] and evaluation of in vitro blood compatibility / A. K. Bajpai // Polymer Internat. – 2005. – V. 54. – P. 304–315.
8. Tang L. Inflammatory responses to implanted polymeric biomaterials: role of surface-adsorbed immunoglobulin G / L. Tang, A. H. Lucas, J. W. Eaton // J. Lab. Clin. Med. – 1993. – V. 122. – P. 292–300.
9. Tang L. Fibrinogen adsorption and host tissue responses to plasma functionalized surfaces / L. Tang, Y. Wu, R. B. Timmons // J. Biomed. Mater. Res. – 1998. – V. 42. – P. 156–163.
10. Heimburg T. Themodynamics of the interaction of proteins with lipid membranes, In Biological Membranes: A molecular perspective from computation and experiment / T. Heimburg, D. Marsh // Birkhauser Boston. – 1996. – P. 405–462.
11. Sankaram M. Protein-lipid interactions with peripheral membrane proteins / M. Sankaram, D. Marsh // In Protein-Lipid Interactions, Elsevier. – 1993. P. 127–162.
12. Bray D. Signaling complexes: biophysical constraints on intracellular communication / D. Bray // Ann. Rev. Biophys. Biomol. Struct. – 1998. – V. 27. – P. 59–75.
13. Protein-induced fusion can be modulated by target membrane lipids through a structural switch at the level of the fusion peptide / E. I. Pecheur, I. Martin, A. Bienvenue [et al.] // J. Biol. Chem. – 2000. – V. 275. – P. 3936–3942.
14. A new model to describe extrinsic protein binding to phospholipid membranes of varying composition: application to human coagulation proteins / G. A. Cutsforth, R. N. Whitaker, J. Hermans, B. R. Lentz // Biochemistry. – 1989. – V. 28. – P. 7453–7461.
15. Cholera toxin assault on lipid monolayers containing ganglioside GM1 / C. E. Miller, J. Majewski, R. Faller [et al.] // Biophys. J. – 2004. – V. 86. – P. 3700–3708.
16. Protein adsorption on supported phospholipid bilayers / K. Glasmӓstar, C. Larsson, F. Höök, B. Kasemo // Colloid Interface Sci. – 2002. – V. 246. – P. 40–47.
17. Gorbenko G. P. Binding of lysozyme to phospholipid bilayers: evidence for protein aggregation upon membrane association / G. P. Gorbenko, V. M. Ioffe, P. K. J. Kinnunen // Biophys. J. – 2007. – V. 93. – P. 140–153.
18. Salafsky J. S. Protein adsorption at interfaces detected by second harmonic generation / J. S. Salafsky, K. B. Eisenthal // J. Phys. Chem. B. – 2000. – V. 104. – P. 7752–7755.
19. Morphological changes of supported lipid bilayers induced by lysozyme: planar domain formation vs. multilayer stacking / V.M. Trusova, G.P. Gorbenko, I. Akopova [et al.] // Colloids Surf. B. – 2010. – V. 80. – P. 219–226.
20. Dynamics of β-lactoglobulin penetration into Langmuir monolayers of 2D condensating phospholipid / V. B. Fainerman, J. Zhao, D. Vollhardt [et al.] // J. Phys. Chem. B. – 1999. – V. 103. – P. 8998–9007.
21. Peng J. B. The structure of Langmuir-Blodgett films of fatty acids and their salts / J. B. Peng, G. T Barnes, I. R. Gentle // Adv. Colloid Interface Sci. – 2001. – V. 91. – P. 163–219.
22. Brockman H. Lipid monolayers: why use half a membrane to characterize protein-membrane interactions / H. Brockman // Curr. Opin. Struct. Biol. – 1999. – V. 9. – P. 438–443.
23. Study of gramicidin A – phospholipid interactions in Langmuir monolayers: analysis of their mechanical, thermodynamical, and electrical properties / M. Weis, M. Vanco, P. Vitovic [et al.] // J. Phys. Chem. B. – 2006. – V. 110. – P. 26272–26278.
24. Interaction of myelin basic protein with phospholipid monolayers: mechanism of protein penetration / E. Polverini, S. Arisi, P. Cavatorta [et al.] // Langmuir. – 2003. – V. 19. – P. 872–877.
25. Molecular organization in protein-lipid film on the water surface studied by x-ray standing wave measurements under total external reflection / S. Zheludeva, N. Novikova, N. Stepina [et al.] // Spectrochim. Acta B. – 2008. – V. 63. – P. 1399–1403.
26. Pethica B. A. The thermodynamics of monolayer penetration at constant area. Part 1 / B. A. Pethica // Trans. Faraday Soc. – 1955. – V. 51. – P. 1402–1411.
27. Anderson P. J. The thermodynamics of monolayer penetration at constant area. Part 1 / P. J. Anderson, B. A. Pethica // Trans. Faraday Soc. – 1956. – V. 52. – P. 1080–1087.
28. Alexander D. M. Use of the Gibbs equation to calculate adsorption into monolayer-covered surfaces / D. M. Alexander, G. T. Barnes // J. Chem. Soc. Faraday Trans. 1. – 1980. – V. 76. – P. 118–125.
29. Thermodynamics of multicomponent monolayers: IV. Monolayer penetration / K. Motomura, Y. Hayami, M. Aratono, R. Matuura // J. Colloid Interface Sci. – P. 333–338.
30. Ter-Minassian-Saraga L. Penetration into insoluble monolayers. 1. A semiopen system behavior / L. Ter-Minassian-Saraga // Langmuir. – 1985. – V. 1. – P. 391–394.
31. Fainerman V. B. Penetration of Langmuir monolayers by soluble amphiphilic molecules / V. B. Fainerman, D. Vollhardt // Langmuir. – 1999. – V. 15. – P. 1784–1790.
32. Sundaram S. Equations for the equilibrium surface pressure increase on the penetration of an insoluble monolayer by soluble surfactant / S. Sundaram, K. J. Stebe // Langmuir. – 1996. – V. 12. – P. 2028–2034.
33. Datwani S. S. Monolayer penetration by a charged amphiphile: equilibrium and dynamics / S. S. Datwani, K. J. Stebe // Colloids Surf. A. – 2001. – V. 192. – P. 109–129.
34. Analysis of the contribution of saturated and polyunsaturated phospholipid monolayers to the binding of proteins / P. Calvez, É. Demers, E. Boisselier, C. Salesse // Langmuir. – 2011. – V. 27. – P. 1373–1379.
35. Influence of the physical state of phospholipid monolayers on protein binding / E. Boisselier, P. Calvez, É. Demers [et al.] // Langmuir. – 2012. – V. 28. – P. 9680–9688.
36. Benga G. Interactions between components in biological membranes and their implication for membrane function / G. Benga, R. Holmes // Progr. Biophys. Mol. Biol. – 1984. – V. 43. – P. 195–257.
37. Jahnig F. Thermodynamics and kinetics of protein incorporation into membranes / F. Jahnig // Proc. Natl. Acad. Sci. USA. – 1983. – V. 80. – P. 3691–3695.
38. Zuckermann M. J. Insertion and pore formation driven by adsorption of protein onto lipid bilayer membrane-water interface / M. J. Zuckermann, T. Heimburg // Biophys. J. – 2001. – V. 81. – P. 2458–2472.
39. Interaction of influenza virus hemagglutinin with a lipid monolayer. A comparison of the surface activities of intact virions, isolated hemagglutinins, and a synthetic fusion peptide / K. N. J. Burger, S. A. Wharton, R. A. Deme1, A. J. Verkleij // Biochemistry. – 1991. – V. 30. – P. 11173–11180.
40. Streptomyces chromofuscus phospholipase D interaction with lipidic activators at the air-water interface / K. E. Kirat, J. P. Chauvet, B. Roux, F. Besson // Biochim. Biophys. Acta. – 2004. – V. 1661. – P. 144–153.
41. Interactions of adriamycin, cytochrome c, and serum albumin with lipid monolayers containing poly(ethylene glycol)-ceramide / H. Zhao, P. M. Dubielecka, T. Soderlund, P. K. J. Kinnunen // Biophys. J. – 2002. – V. 83. – P. 954–967.
42. Thakur G. Surface chemistry of Alzheimer’s disease: a Langmuir monolayer approach / G. Thakur, M. Micic, R. M. Leblanc // Colloids Surf. B. – 2009. – V. 74. – P. 436–456.
Цитовано
Як цитувати
Trusova, V. M. (1). Моделювання адсорбції білків на поверхню ліпідного моношару. Біофізичний вісник, 1(29). вилучено із https://periodicals.karazin.ua/biophysvisnyk/article/view/2326
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