The sequence of preferential coupling of ligands with hyaluronidase is elicited in our study making it possible to evaluate the feasibility of achieving experimental selective modification of the enzyme (possibly noncovalently or covalently, for instance, with chondroitin sulfate trimers on centers cs7, cs1, cs5) for potential experimental production of stabilized forms of the enzyme. The importance of ligand binding for the regulation of the functioning of the enzyme and the presence of a diverse and multicomponent microenvironment of the biocatalyst is noted. The binding of chondroitin trimers (on centers cs2, cs4, cs7, cs8 or cs1, cs2, cs4, cs7, cs8) decreased the inhibition of the enzyme by tetramer heparin. As a result of this, the inactivation and stabilization of the enzyme globule are observed, and a change in its inhibition by heparin. The reported impact was due to electrostatic noncovalent interactions (without specific binding to the active site), causing noticeable conformational changes in the molecule biocatalyst/enzyme. Exploratory computational consideration of the interaction of a 3D model of bovine testicular hyaluronidase (BTH) with short chain glycosaminoglycan ligands demonstrated the diversity and significance of their effect on the structure of the enzyme. The computational study of a 3D model of the hyaluronidase interaction with shortchain glycosaminoglycan ligands demonstrated the diversity and significance of their reaction on enzyme structure.
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