Localization of the E. coli Dps protein molecules in a silicon wires under removal of residual salt
Abstract
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.
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