A comparative asessment of the sorption activity of silver (Ag) nanoparticles (SNPs) on the surface of biodegradable and non-degradable fibers of the suture fibers has been carried out. The predominance of the desorption process from the surface of fibers of both types has been elucidated during the first day after fiber incubation in gels with the SNPs. At the same time, a pronounced sorption process was noted on the surface of the non-absorbable Polyester thread within 24 hours after its incubation in the Agrogel silver nanoparticle preparation and in the absorbable Dexon material exposed to the gel composition containing the SNPs synthesized ex tempore. The observed differences are caused by both the physico-chemical characteristics of the thread surface and the dependence on the size range of the employed silver nanoparticles.

The specific features of the sorption activity of silver nanoparticles (AgNPs) on biodegradable polymers of natural (collagen) and artificial (polyamide 6.6) origin have been established. The ability has been demonstrated for resorbable fibers of natural origin to more actively adsorb AgNPs with sizes from 1 to 10 nm during the first hour and stronger hold them on the surface during the first day of exposure to argogel. During the first hour of incubation of these polymers in a gel composition containing AgNPs obtained by the method of cavitation-diffusion photochemical reduction, their higher sorption activity was revealed in the size range from 1 to 10 nm in relation to the polyfilament synthetic material. After 24 h of exposure, a significant increase in the fraction of small AgNPs already on collagen fibers was observed, which was also accompanied by a significantly lower (19 times) content of AgNPs with a diameter above 40 nm on the catgut.

Abstract—It is established that a medium with a reduced content of deuterium has no effect on the secondary structure of horseradish peroxidase and bovine serum albumin and caused no conformational changes in the structures of these proteins. The placement of these proteins in a buffer solution prepared based on deuterium-depleted water led to a decrease in the intensity of intrinsic tryptophan fluorescence, while the circular dichroism spectra remained virtually unchanged. A decrease in the content of deuterium in the reaction medium led to a decrease in the activity of the peroxidase oxidation reaction of o-dianisidine and luminal with hydrogen peroxide.

The physical regularities that lead to isotope fractionation and to the accumulation of certain isotope forms in the intercellular and intracellular space at various levels of biological objects were studied. A new hypothesis of fractionation of stable isotopes in biological objects through the neutron effect was discussed. The following feature is noted: it is very likely that the development of isotope shock in living beings is observed mainly in the presence of covalent bonds between atoms with an uncompensated neutron. One possible explanation for this phenomenon can be associated with a change in the physical parameters of the following events: the interactions of the magnetic moments of valence electrons with the magnetic moments of atomic nuclei and the interactions of magnetic moments of atomic nuclei, which result in a change in the distance between atomic nuclei.