Abstract
1. <span style=font-size:11.0pt;mso-ansi-language: EN-US>Abstract Computational analysis of molecular docking of 3D model of bovine testicular hyaluronidase in silico with a trimer (hexasaccharide) chondroitin sulfate and tetramer (octasaccharide) heparin has demonstrated eight significant binding sites (cs1-cs8) for these ligands. Interactions with heparin that inactivates the enzyme and protective effects of chondroitin sulfate were examined. Binding sites have been identified which are critical for stabilization of the protein structure after chondroitin sulfate binding: at positions cs2, cs4, cs7 and cs8 or cs1, cs2, cs4, cs7 and cs8. Occupation of these sites is theoretically sufficient for prevention of irreversible molecular deformations after heparin inclusion into active site. The presence of sensitivity sites on hyaluronidase globule indicates the possibility of regulating the enzyme function via coupling glycosaminoglycan ligands thus initiating delicate/fine formation of effective electrostatic potential. Interactions between glycosaminoglycan ligands and hyaluronidase are based primarily on electrostatic forces. 2. <span style=font-size:11.0pt;mso-ansi-language: EN-US>Keywords: <span style=font-size:10.0pt;mso-ansi-language: EN-US>Bovine Testicular Hyaluronidase; Chondroitin Sulfate; Docking; Glycosaminoglycan Ligands; Heparin
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