LA FASE ESPONJA COMO SISTEMA BIOMIMÉTICO PARA CRISTALIZAR PROTEÍNAS DE MEMBRANA
DOI:
https://doi.org/10.36790/epistemus.v10i20.17Keywords:
Fase esponja, biomimética, cristalización, proteinasAbstract
En este trabajo se describe de manera general la importancia de la cristalización de proteínas para realizar experimentos de difracción de rayos X que permitan dilucidar la estructura terciaria de dichas biomoléculas. En particular, se expone que la cristalización de proteínas de membrana requiere métodos especiales de preparación de la matriz de cristalización puesto que se debe “mimetizar” el ambiente hidrofóbico de la proteína en la membrana. De esta manera, el trabajo se centra en algunas propiedades de la fase líquida de membranas denominada “fase esponja”, cuya característica principal es una estructura membranar compleja conectada en tres dimensiones. Debido a su microestructura, la fase esponja es transparente e isotrópica, además de presentar baja viscosidad en las membranas. Estas características convierten a la fase esponja en un medio “biomimético” potencialmente útil para cristalizar proteínas de membrana.
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References
Shen, Y. X., Saboe, P. O., Sines, I. T., Erbakan, M., & Kumar, M.. Biomimetic membranes: a review. Journal of Membrane Science, 454, 359-381, 2014. DOI: https://doi.org/10.1016/j.memsci.2013.12.019
Whitford, D. Proteins: structure and function. John Wiley & Sons, 2013.
Darby, N. J., & Creighton, T. E. Protein structure (pp. 1-41). Oxford, UK: IRL Press at Oxford University Press, 1993.
http://www.rscb.org/pdb/static.do?p=general_information/about_pdb/nature_of_3d_structural_dat.html
Schnell, J. R., & Chou, J. J. Structure and mechanism of the M2 proton channel of influenza A virus. Nature, 451(7178), 591-595, 2008. DOI: https://doi.org/10.1038/nature06531
Maldonado, A., Urbach, W., Ober, R., & Langevin, D. Swelling behavior and local topology of an L 3 (sponge) phase. Physical Review E, 54(2), 1774-1778, 1996. DOI: https://doi.org/10.1103/PhysRevE.54.1774
Maldonado, A., Ober, R., Gulik-Krzywicki, T., Urbach, W., & Langevin, D. The sponge phase of a mixed surfactant system. Journal of colloid and interface science, 308(2), 485-490, 2007. DOI: https://doi.org/10.1016/j.jcis.2007.01.012
Ridell, A., Ekelund, K., Evertsson, H., & Engström, S. On the water content of the solvent/monoolein/water sponge (L3) phase. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 228(1), 17-24, 2003. DOI: https://doi.org/10.1016/S0927-7757(03)00299-1
Kulkarni, C. V., Wachter, W., Iglesias-Salto, G., Engelskirchen, S., & Ahualli, S. Monoolein: a magic lipid?. Physical Chemistry Chemical Physics, 13(8), 3004-3021, 2011. DOI: https://doi.org/10.1039/C0CP01539C
Gambin, Y., Lopez-Esparza, R., Reffay, M., Sierecki, E., Gov, N. S., Genest, M., Urbach, W. Lateral mobility of proteins in liquid membranes revisited. Proceedings of the National Academy of Sciences of the United States of America, 103(7), 2098-2102, 2006. DOI: https://doi.org/10.1073/pnas.0511026103
Maldonado, A., Urbach, W., & Langevin, D. Surface self-diffusion in L3 Phases. The Journal of Physical Chemistry B, 101(41), 8069-8073, 1997. DOI: https://doi.org/10.1021/jp964039v
Li, D., Shah, S. T., & Caffrey, M. Host lipid and temperature as important screening variables for crystallizing integral membrane proteins in lipidic mesophases. Trials with diacylglycerol kinase. Crystal growth & design, 13(7), 2846-2857, 2013. DOI: https://doi.org/10.1021/cg400254v
Caffrey, M. Crystallizing membrane proteins for structure-function studies using lipidic mesophases. In Advancing Methods for Biomolecular Crystallography (pp. 33-46). Springer Netherlands, 2013. DOI: https://doi.org/10.1007/978-94-007-6232-9_4
Caffrey, M., Li, D., & Dukkipati, A. Membrane protein structure determination using crystallography and lipidic mesophases: recent advances and successes. Biochemistry, 51(32), 6266-6288, 2012. DOI: https://doi.org/10.1021/bi300010w
Joseph, J. S., Liu, W., Kunken, J., Weiss, T. M., Tsuruta, H., & Cherezov, V. Characterization of lipid matrices for membrane protein crystallization by high-throughput small angle X-ray scattering. Methods, 55(4), 342-349, 2011. DOI: https://doi.org/10.1016/j.ymeth.2011.08.013
Johansson, L. C., Arnlund, D., White, T. A., Katona, G., DePonte, D. P., Weierstall, U., & Schlichting, I. Lipidic phase membrane protein serial femtosecond crystallography. Nature Methods, 9(3), 263-265, 2012. DOI: https://doi.org/10.1038/nmeth.1867
Oka, T., & Hojo, H. Single Crystallization of an Inverse Bicontinuous Cubic Phase of a Lipid. Langmuir, 30(28), 8253-8257, 2014. DOI: https://doi.org/10.1021/la502002r
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