[Parametabolism as Non-Specific Modifier of Supramolecular Interactions in Living Systems].

As it became known recently, in addition to the enzyme (enzymes and/or ribozymes) in living organisms occur a large number of ordinary chemical reactions without the participation of biological catalysts. These reactions are distinguished by low speed and, as a rule, the irreversibility. For example, along with diabetes mellitus, glycation and fructosilation of proteins are observed resulted in posttranslational modification with the low- or nonfunctioning protein formation which is poorly exposed to enzymatic proteolysis and therefore accumulates in the body. In addition, the known processes such as the nonenzymatic carbomoylation, pyridoxylation and thiamiation proteins. There is a reasonable basis to believe that alcoholic injury also realized through parametabolic secondary metabolites synthesis such as acetaldehyde. At the same time, the progress in supramolecular chemistry proves that in biological objects there is another large group ofparametabolic reactions caused by the formation of supramolecular complexes. Obviously, known parameterizes interactions can modify the formation of supramolecular complexes in living objects. These processes are of considerable interest for fundamental biology and fundamental and practical medicine, but they remain unexplored due to a lack of awareness of a wide range of researchers.

[The comparative analysis of various amyloid models].

Considered natural and experimental amyloidosis models in the existing theories context and known amyloidogenesis mechanisms. Available clinical and experimental observations indicate that the opinion of a fatal incurable amyloidosis wrong. It is shown that there is a significant amount of experimental easily replicable amyloidosis models, which may be used for practicing the treatment methods of this pathology. We offer an amyloidosis models classification: natural (animal models with generic amyloidosis), cell clones, artificial (infectious, protein, etc.). Based on the analysis of amyloidosis existing models concluded--none of the accepted in the scientific the theories community for amyloid building does not combine or explains all known facts about the amyloidogenesis mechanisms. It is assumed that there is a proteins group, the beta-sheet structure, which are potentially capable of amyloid conformation building. It is assumed that beta-sheets of these proteins have similar amino acid composition. The condition for the amyloid building conformation is getting too much protein in sufficient quantities in an uncharacteristic place where the ionic strength of the tissue fluid is such that it promotes the amyloid building conformation. It is assumed that an unfortunate amount of ionic strength environment amyloid protein is provided by polysaccharides, tubulins proteins and ionized silicon.