Localization of the E. coli Dps protein molecules in a silicon wires under removal of residual salt
The work is related to the removal of residual salts in hybrid structures formed as a result of silicon wires arrays combining with a nanomaterial of natural origin – bacterial ferritin-like protein Dps. The study of the morphology and composition of the surface and the bulk part of the hybrid structure as a result of combination and subsequent washing in water was carried out.
The method of metal-assisted wet chemical etching was used to obtain silicon wires arrays. To obtain recombinant protein, Escherichia coli BL21*(DE3) cells with chromatographic purification were used as producers. The combination of silicon wires with protein molecules was carried out by layering them in laboratory conditions, followed by drying. The residual salt found earlier in the hybrid material was removed by washing in water. The resulting hybrid material was studied by scanning electron microscopy and X-ray photoelectron spectroscopy. A well-proven complementary combination of scanning electron microscopy and X-ray photoelectron spectroscopy together with ion etching was used to study the morphology of the hybrid material “silicon wires – bacterial protein Dps” and the composition with physico-chemical state respectively.
In arrays of silicon wires with a wire diameter of about 100 nm and a distance between them from submicron to nanometer sizes, protein was found as a result of layering and after treatment in water. At the same time, the amount of residual NaCl salt is minimized on the surface of the hybrid structure and in its volume.
The obtained data can be used in the development of coating technology for the silicon wires developed surface available for functionalization with controlled delivery of biohybrid material.
Behrens S. Synthesis of inorganic nanomaterials mediated by protein assemblies. Journal of Materials Chemistry. 2008;18: 3788–3798. https://doi.org/10.1039/B806551A
Andrews S. C. Iron storage in bacteria. Advances in Microbial Physiology. 1998;40: 281–351. https://doi.org/10.1016/S0065-2911(08)60134-4
Harrison P. M., Arosio P. The ferritins: molecular properties, iron storage function and cellular regulation. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1996;1275(3): 161–203. https://doi.org/10.1016/0005-2728(96)00022-9
Massover W. H. Ultrastructure of ferritin and apoferritin: A review. Micron. 1993;24(3): 389–437. https://doi.org/10.1016/0968-4328(93)90005-L
Theil E. C. The ferritin family of iron storage proteins. Advances in enzymology and related areas of molecular biology. 1990;63: 421–449. https://doi.org/10.1002/9780470123096.ch7
Antipov S., Turishchev S., Purtov Yu., … Ozoline O. The oligomeric form of the Escherichia coli Dps 3 protein depends on the availability of iron ions. Molecules. 2017;22(11): 1904. https://doi.org/10.3390/molecules22111904
Zhang Y., Fu J., Chee S. Y., Ang E. X., Orner B. P. Rational disruption of the oligomerization of the mini-ferritin E. coli DPS through protein–protein interface mutation. Protein Science. 2011;20(11): 1907–1917. https://doi.org/10.1002/pro.731
Antipov S. S., Pichkur E. B., Praslova N. V., … Turishchev S. Yu. High resolution cryogenic transmission electron microscopy study of Escherichia coli Dps protein: first direct observation in quasinative state. Results in Physics. 2018;11: 926–928. https://doi.org/10.1016/j.rinp.2018.10.059
Parinova E. V., Antipov S. S., Belikov E. A., … Turishchev S. Yu. TEM and XPS studies of bio-nanohybrid material based on bacterial ferritin-like protein Dps. Condensed Matter and Interphases. 2022;24(2): 265–272. https://doi.org/10.17308/kcmf.2022.24/9267
Parinova E. V., Antipov S. S., Belikov E. A., Kakuliia I. S., Trebunskikh S. Y., Turishchev S. Y., Sivakov V. Localization of DPS protein in porous silicon nanowires matrix. Results in Physics. 2022;35, 105348. https://doi.org/10.1016/j.rinp.2022.105348
Parinova E. V., Antipov S. S., Sivakov V., … Turishchev S. Yu. Localization of the E. coli Dps protein molecules in a silicon wires matrix according to scanning electron microscopy and X-ray photoelectron spectroscopy. Condensed Matter and Interphases. 2023;25(2): 207–217. https://doi.org/10.17308/kcmf.2023.25/1110
Sivakov V. A., Brönstrup G., Pecz B., Berger A., Radnoczi G. Z., Krause M., Christiansen S. H. Realization of vertical and zigzag single crystalline silicon nanowire architectures. The Journal of Physical Chemistry C. 2010;114: 3798–3803. https://doi.org/10.1021/jp909946x
Lo Faro M. J., Leonardi A. A., D’Andrea C., … Irrera A. Low cost synthesis of silicon nanowires for photonic applications. Journal of Materials Science: Materials in Electronics. 2020;31: 34–40. https://doi.org/10.1007/s10854-019-00672-y
Lebedev A. M., Menshikov K. A., Nazin V. G., Stankevich V. G., Tsetlin M. B., Chumakov R. G. NanoPES photoelectron beamline of the Kurchatov Synchrotron Radiation Source. Journal of Surface Investigation: X-ray, Synchrotron and Neutron Techniques. 2021;15(5): 1039–1044. https://doi.org/10.1134/S1027451021050335
John F. Moulder handbook of X-ray photoelectron spectroscopy. Minnesota: Published by Perkin-Elmer Corporation Physical Electronics Division United States of America; 1992. 261 p.
Handbook of the elements and native oxide. XPS International, Inc.; 1999. 658 p.
Hüfner S. (ed.). Very high resolution photoelectron spectroscopy. In: Lecture Notes in Physics. Berlin: Springer; 2007. https://doi.org/10.1007/3-540-68133-7
Copyright (c) 2023 Condensed Matter and Interphases
This work is licensed under a Creative Commons Attribution 4.0 International License.