ABSTRACT
Wide-pore proteinaceous freeze-thaw spongy gels were synthesized via the cryotropic gelation technique using the bovine blood serum or its diluted solutions as the protein-containing precursors. The feed systems also included the denaturant (urea) and the thiol-reductant (cysteine). The gel-fraction yield decreased and the swelling degree of the walls of macropores in such heterophase matrices increased with decreasing the initial protein concentration. The optimum freezing temperature was found to be within a rather narrow range from -15 to -20 °C. In this case, the average size of the macropores in the resultant cryogels was 90-110 µm. The suitability of such soft wide-pore gel materials for the application as the carriers of peptide bioregulators was demonstrated in the in vitro experiments, when the posterior segments of the Pleurodeles waltl adult newts' eyes were used as a model biological target. It was shown that a statistically reliable protective effect on the state of the sclera, vascular membrane and retinal pigment epithelium, as well as on the viability of fibroblasts, was inherent in the proteinaceous cryogels loaded with the peptide bioregulator (Viophtan-5™) isolated from the bovine eye sclera.
ABSTRACT
The influence of temperature and chaotropic agents on the spatial organization of the peptide-protein complex isolated from cattle sclera at the level of secondary structure was studied by UV, CD spectroscopy, and dynamic light scattering. It is shown that this complex has high conformational thermostability. The point of conformational thermal transition (65 °C) was determined, after which the peptide-protein complex passes into a denatured stable state. It was found that the peptide-protein complex in aqueous solutions forms thermostable nanosized particles. It was shown that the peptide-protein complex isolated from cattle sclera shows the properties of chaperone, an inhibitor of model protein aggregation induced by dithiothreitol.