Publications by authors named "Ludmila Semenycheva"

New photocatalytic materials based on complex oxides and a widely used and cheap polymer (PMMA) have been prepared. Among complex oxides previously investigated, the following have been used-RbTeWO, CsTeMoO, CsVTeO, NaVMoO, KVMoO. For comparison, the binary oxides TiO and WO were used.

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Graft copolymerization of methyl methacrylate onto cod collagen was carried out under visible light irradiation (λ = 400-700 nm) at 20-25 °C using the RbTeWO, CsTeMoO, and RbNbTeO complex oxides with β-pyrochlore structure as photocatalysts. The as-prepared materials were characterized by X-ray diffraction, scanning electron microscopy, and UV-Vis diffuse reflectance spectroscopy. It was also found that RbNbTeO with β-pyrochlore structure was not able to photocatalyze the reaction.

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Biopolymers, in particular collagen and fibrinogen, are the leading materials for use in tissue engineering. When developing technology for scaffold formation, it is important to understand the properties of the source materials as well as the mechanisms that determine the formation of the scaffold structures. Both factors influence the properties of scaffolds to a great extent.

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Enzymatic hydrolysis of native collagen and fibrinogen was carried out under comparable conditions at room temperature. The molecular weight parameters of proteins before and after hydrolysis by thrombin were monitored by gel-penetrating chromatography (GPC). An analysis of the experiment results shows that the molecular weight parameters of the initial fibrinogen (Fn) and cod collagen (CC) are very similar.

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At present there is a growing need for tissue engineering products, including the products of scaffold-technologies. Biopolymer hydrogel scaffolds have a number of advantages and are increasingly being used to provide means of cell transfer for therapeutic treatments and for inducing tissue regeneration. This work presents original hydrogel biopolymer scaffolds based on a blood plasma cryoprecipitate and collagen and formed under conditions of enzymatic hydrolysis.

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