Biofilms are complex systems that have high cell density, ranging from 10 8 to 10 11 cells g-1

The selectivity of serine proteinases action is mediated by high-specifice binding of the proper parts of the protein substrate. Among such protein targets a special place belongs to the areas of functionally conditioned interaction with the active center of the enzyme. Their sharp difference in enzyme affinity is due to synchronous interaction of the binding and allosteric sites of the active site with specific amino acid residues of the substrate that are adequate in specificity and placed in the proper conformation. This paper is devoted to the consideration of the manifestation of allosteric erosion of primary specificity of serine proteinases. Examples of such effects as well as the possibilities of their application are discussed.

Abstract. The formation in β-structured protein aggregates in tissues and fluids of the body is one of the most dangerouse complications of various diseases. The most famous of them are amyloidoses, but they such deposits are observed at other, much more widespread, diseases. The generally accepted approach to amyloids’detectionis based on  high-specific coloring by Congo Red dye. However, the Abbe's diffraction limit excludes the seeing of the objects smaller than 0.61 wavelengths (about 240 nm). Such nanoscale formations are capable to disrup the functioning of surrounding tissues, to causethe complications and recurrences of the disease, and to pass through biological barriers with the following accumulation in body’s fluids. It’s likely that these conditions are the cause of the urinary congophilia, that is associated with preeclampsia at pregnancy and chronic kidney disease. Nor the less suspicious object is the Bens-Jones protein that appears in the urine at multiple myeloma and some other diseases, which are in more or less extent,are related to the disturbance of protein metabolism. The purpose of this study was to clarify the aggregate state of the Bens-Jones protein as a possible β-structured supramolecular associate. Methods.The subject of the study was the freshly received urine from a patient with multiple myeloma. The presence of the Bens-Jones protein was checked by thermopacification of the acidified sample. For control, the urine was used by a healthy person with the addition of certain amounts of human serum albumin ("Reanal", Hungary) with a concentration of 0, 0.01, 0.1 and 1%. Result. The obtained data testify to the appropriateness of such a point of view and create preresquites for the expanding of diagnostic possibilities. Conclusions.The results obtained during the study testify to the peculiarity of the structure of the Bens-Jones protein, which is nano-sized beta-structured supramolecular

Summary. Aim: To evaluate the presence of the aggregated proteins in malignant and benign neoplasms for clarifying the role of impaired protein metabolism in the formation of the altered tissues. Object and Methods: The histological specimens prepared from the operative materials of 196 patients with different forms of malignant and benign neoplasms were stained with Congo red and Thioflavin T and studied under the light and polarization microscope. Results: The various forms of β-stacked protein aggregates (β-SPA) inclusions were detected in amyloids, keloid tissue, benign polyps, and several malignant tumors. Conclusion: The formation of non-functional protein aggregates proves the complex character of the impairment of protein metabolism resulting in local or systemic accumulation of secondary protein toxins results in β-SPA formation as the self-sustaining complex of parametabolic processes. The β-SPA formation is of considerable interest since their properties lead to the impairment of the normal physiological processes in adjacent tissues ensuring the chronic course of the pathology.

the ability of various metal ions to form complexes with proteins leads to the denaturation of the latter and the development of immune response. Such hapten effects cause the well-known phenomenon of nickel-allergic contact dermatitis. No less typical are side effects of gadolinium compounds, that are used as contrasts for magnetic resonance imaging, but cause the development of fibrosis. In both cases an important role belongs to the interaction of metal ions with collagen structures. The aim of our study was to compare in vitro effects of copper and nickel ions on destabilized products of collagen cleavage. Significant difference between these metals in their ability to induce aggregation at close to physiological pH values was shown. The influence on the aggregative process of the acidification of the medium was revealed. It was shown that destabilization of protein structure leads to the formation of highly stabilized β-stacked protein aggregates. Comparison of the obtained experimental data with the  literature ones makes it possible to approach the understanding of individual mechanisms of toxic effects of metal ions on the human body.