[Dependence of the efficiency of cell growth on biosynthetic medical materials on the microstructure of their surface].

The efficiency of a novel class of biosynthetic wound dressings in wich natural and synthetic polymeric components are not arranged in layers but are in a unified structure, i. e., form a new composite material, has been studied.

[Nanocomposite regeneration systems for wound healing].

The regeneration system "Biokol" based on the principles of combining the synthetic and natural biopolymers has been investigated. The wound dressing consists of "large" (200-250 nm) particles of a synthetic biopolymer and a gel component, which constitutes "small" polysaccharide elements 10-20 nm in size. The system can be used both separately and in combination with the gel complex and cell cultures.

[A study of the effect of irradiation hardness on the properties of the fluoropolymeric matrix modified by polyanionic biologically active substances].

The properties of a synthetic substrate responsible for the behavior of substrate-dependent cells in the culture were studied. The effect of the composition of a system water-soluble biopolymer (sodium alginate or methyl cellulose)-synthetic latex SKF-26 and the effect of various types of radiations on its biophysical properties were studied. The results obtained indicate that the addition of water-soluble biopolymeric additives to synthetic polymeric films improves the adhesion of cells to the substrate, the adhesion being closely related to the concentration of additives.

[Formation of collagen type I fibrils in vitro].

The assembly of collagen fibrils as a function of temperature and collagen concentration was studied. It was shown that temperature increases from 25 to 35 degrees C, the degree of ordering of collagen fibrils increases 1.5-fold at collagen concentration above 1 mg/ml and 2-fold at low collagen concentration.

[Self-assembly of collagen type I molecules without telopeptides].

The effect of temperature on the kinetics of formation of fibrils from rat tail collagen molecules devoid of telopeptides was studied. It was shown that the rats of fibril formation at 30 and 35 degrees C increases five- and eightfold, respectively, as compared with that at 25 degrees C. It was found that enthalpy of fibril denaturation at 30 degrees C is maximal for the collagen both with intact telopeptides and devoid of telopeptides.