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Volume 2017, Article ID 1542156, 9 pages
https://doi.org/10.1155/2017/1542156
Research Article

Effects of Concentration and Surface Pressure on MBP Interaction with Cholesterol in Langmuir Films

School of Physics and Information Technology, Shaanxi Normal University, Xi’an 710062, China

Correspondence should be addressed to Changchun Hao; nc.ude.unns@nuhcgnahcoah and Runguang Sun; nc.ude.unns@gnaugnurnus

Received 9 July 2017; Revised 31 August 2017; Accepted 12 September 2017; Published 7 November 2017

Academic Editor: Guosong Wu

Copyright © 2017 Lei Zhang et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. D. H. Mauch, K. Nägier, S. Schumacher et al., “CNS synaptogenesis promoted by glia-derived cholesterol,” Science, vol. 294, no. 5545, pp. 1354–1357, 2001. View at Publisher · View at Google Scholar · View at Scopus
  2. F. Liu, X. Zhang, C. Lu et al., “Non-specific lipid transfer proteins in plants: Presenting new advances and an integrated functional analysis,” Journal of Experimental Botany, vol. 66, no. 19, pp. 5663–5681, 2015. View at Publisher · View at Google Scholar · View at Scopus
  3. A. Ulman, An Introduction to Ultrathin Organic Films: from Langmuir-Blodgett to Self-Assembly, Academic Press, London, UK, 1991.
  4. J. M. Boggs and M. A. Moscarello, “Structural organization of myelin: role of lipid-protein interaction determined in mole system,” in Lipid-Protein Interaction, P. C. Jost, O. H. Griffith, and P. C. Jost, Eds., vol. 2, pp. 1–51, Wiley, New York, NY, USA.
  5. P. Riccio, L. Masotti, P. Cavatorta et al., “Myelin basic protein ability to organize lipid bilayers: Structural transition in bilayers of lisophosphatidylcholine micelles,” Biochemical and Biophysical Research Communications, vol. 134, no. 1, pp. 313–319, 1986. View at Publisher · View at Google Scholar · View at Scopus
  6. P. Morell, Myelin, Springer US, Boston, Mass, USA, 2nd edition, 1984. View at Publisher · View at Google Scholar
  7. J. M. Boggs, “Myelin basic protein: A multifunctional protein,” Cellular and Molecular Life Sciences, vol. 63, no. 17, pp. 1945–1961, 2006. View at Publisher · View at Google Scholar · View at Scopus
  8. G. Harauz, V. Ladizhansky, and J. M. Boggs, “Structural polymorphism and multifunctionality of myelin basic protein,” Biochemistry, vol. 48, no. 34, pp. 8094–8104, 2009. View at Publisher · View at Google Scholar · View at Scopus
  9. J. Sedzik and D. A. Kirschner, “Is myelin basic protein crystallizable?” Neurochemical Research, vol. 17, no. 2, pp. 157–166, 1992. View at Publisher · View at Google Scholar · View at Scopus
  10. M. E. Bechler, L. Byrne, and C. Ffrench-Constant, “CNS Myelin Sheath Lengths Are an Intrinsic Property of Oligodendrocytes,” Current Biology, vol. 25, no. 18, Article ID 12199, pp. 2411–2416, 2015. View at Publisher · View at Google Scholar · View at Scopus
  11. E. Domènech-Estévez, H. Baloui, X. Meng et al., “Akt regulates axon wrapping and myelin sheath thickness in the PNS,” The Journal of Neuroscience, vol. 36, no. 16, pp. 4506–4521, 2016. View at Publisher · View at Google Scholar · View at Scopus
  12. C. M. Rosetti, B. Maggio, and N. Wilke, “Micron-scale phase segregation in lipid monolayers induced by myelin basic protein in the presence of a cholesterol analog,” Biochimica et Biophysica Acta (BBA) - Biomembranes, vol. 1798, no. 3, pp. 498–505, 2010. View at Publisher · View at Google Scholar · View at Scopus
  13. N. S. Murthy, D. D. Wood, and M. A. Moscarello, “X-ray scattering studies of a model complex of lipid and basic protein of myelin,” BBA - Biomembranes, vol. 769, no. 2, pp. 493–498, 1984. View at Publisher · View at Google Scholar · View at Scopus
  14. I. R. Bates, J. M. Boggs, J. B. Feix, and G. Harauz, “Membrane-anchoring and charge effects in the interaction of myelin basic protein with lipid bilayers studied by site-directed spin labeling,” The Journal of Biological Chemistry, vol. 278, no. 31, pp. 29041–29047, 2003. View at Publisher · View at Google Scholar · View at Scopus
  15. M. B. Sankaram, P. J. Brophy, and D. Marsh, “Spin-label ESR studies on the interaction of bovine spinal cord myelin basic protein with dimyristoylphosphatidylglycerol dispersions,” Biochemistry, vol. 28, no. 25, pp. 9685–9691, 1989. View at Publisher · View at Google Scholar · View at Scopus
  16. C. M. Rosetti, B. Maggio, and R. G. Oliveira, “The self-organization of lipids and proteins of myelin at the membrane interface. Molecular factors underlying the microheterogeneity of domain segregation,” Biochimica et Biophysica Acta (BBA) - Biomembranes, vol. 1778, no. 7-8, pp. 1665–1675, 2008. View at Publisher · View at Google Scholar · View at Scopus
  17. J. J. Hulce, A. B. Cognetta, M. J. Niphakis, S. E. Tully, and B. F. Cravatt, “Proteome-wide mapping of cholesterol-interacting proteins in mammalian cells,” Nature Methods, vol. 10, no. 3, pp. 259–264, 2013. View at Publisher · View at Google Scholar · View at Scopus
  18. G. E. Deibler, L. F. Boyd, and M. W. Kies, “Proteolytic activity associated with purified myelin basic protein,” in Experimental Allergic Encephalomyelitis: A Useful Model for Multiple Sclerosis, E. C. Alvord Jr., M. W. Kies, and A. J. Suckling, Eds., pp. 249–256, Liss, New York, NY, USA, 1984. View at Google Scholar
  19. M. Vrânceanu, K. Winkler, H. Nirschl, and G. Leneweit, “Surface rheology of monolayers of phospholipids and cholesterol measured with axisymmetric drop shape analysis,” Colloids and Surfaces A: Physicochemical and Engineering Aspects, vol. 311, no. 1-3, pp. 140–153, 2007. View at Publisher · View at Google Scholar · View at Scopus
  20. J. J. Collins and M. C. Phillips, “The stability and structure of cholesterol-rich codispersions of cholesterol and phosphatidylcholine,” Journal of Lipid Research, vol. 23, no. 2, pp. 291–298, 1982. View at Google Scholar · View at Scopus
  21. E. Falck, M. Patra, M. Karttunen, M. T. Hyvönen, and I. Vattulainen, “Impact of cholesterol on voids in phospholipid membranes,” The Journal of Chemical Physics, vol. 121, no. 24, pp. 12676–12689, 2004. View at Publisher · View at Google Scholar · View at Scopus
  22. G. Cermenati, N. Mitro, M. Audano et al., “Lipids in the nervous system: From biochemistry and molecular biology to patho-physiology,” Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, vol. 1851, no. 1, pp. 51–60, 2015. View at Publisher · View at Google Scholar · View at Scopus
  23. M. A. Alsina, A. Ortiz, D. Polo, F. Comelles, and F. Reig, “Synthesis and study of molecular interactions between phosphatidyl choline and two laminin derived peptides hydrophobically modified,” Journal of Colloid and Interface Science, vol. 294, no. 2, pp. 385–390, 2006. View at Publisher · View at Google Scholar · View at Scopus
  24. C. Hao, L. Zhang, R. Sun, J. Yang, and G. He, “Interaction between ganglioside GM1 and diosgenin in langmuir monolayers at the air/water interface,” Scanning, vol. 36, no. 2, pp. 218–223, 2014. View at Publisher · View at Google Scholar · View at Scopus
  25. M. J. Sánchez-Martín, M. A. Busquets, V. Girona, I. Haro, M. A. Alsina, and M. Pujol, “Effect of E1(64-81) hepatitis G peptide on the in vitro interaction of HIV-1 fusion peptide with membrane models,” Biochimica et Biophysica Acta (BBA) - Biomembranes, vol. 1808, no. 9, pp. 2178–2188, 2011. View at Publisher · View at Google Scholar · View at Scopus
  26. A. A. Hidalgo, A. S. Pimentel, M. Tabak, and O. N. Oliveira Jr., “Thermodynamic and infrared analyses of the interaction of chlorpromazine with phospholipid monolayers,” The Journal of Physical Chemistry B, vol. 110, no. 39, pp. 19637–19646, 2006. View at Publisher · View at Google Scholar · View at Scopus
  27. P. Wydro, B. Krajewska, and K. Ha̧c-Wydro, “Chitosan as a lipid binder: A langmuir monolayer study of chitosan-lipid interactions,” Biomacromolecules, vol. 8, no. 8, pp. 2611–2617, 2007. View at Publisher · View at Google Scholar · View at Scopus