Influence of glycosaminoglycan derivative on hyaluronidase function. Experimental study of effect on native and modified enzyme

The computational study of 3D-model hyaluronidase interaction with shortchain glycosaminoglycan ligands had performed demonstrating the diversity and significance of their reaction on enzyme structure. The purpose of this review was evolution of limiting enzyme functioning interactions (impact on stability, biocatalyst activity) with grounding of recommendations for experimental modification of hyaluronidase for obtaining of its derivative of medicine destination (according the results of theoretical researches). The analysis was performed on databases of PubMed, Web of Science, MedLine, E-library in frames last 15 years. The binding of chondroitin trimers (on centers cn6, cn3, cn1) to hyaluronidase molecular surface increased the enzyme stability, binding of chondroitin sulfate trimers (on centers cs2, cs4, cs7, cs8 or cs1, cs2, cs4, cs7, cs8) decreased the inhibition of enzyme by tetramer heparin. It should be noted the importance of ligand binding for regulation of enzyme functioning and existence of multiform and multicomponent microenvironment of enzyme. The sequence of preferable coupling of ligands with hyaluronidase is elicited in our study and with its help was evaluate reality of experimental selective modification of enzyme (possibly noncovalent or covalently, for instance, with chondroitin sulfate trimers on centers cs7, cs1, cs5) for experimental obtaining of stabilized enzyme forms. The perspective approaches for this aim may be the noncovalent reaction on hyaluronidase by chondroitin or chondroitin sulfate trimers as well covalent modification of biocatalyst by chondroitin sulfate trimers.

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Influence of glycosaminoglycan derivative on hyaluronidase function. Experimental study of effect on native and modified enzyme

Cited by 4 publications

References 14 publications

Theoretical Grounding and Formation of Experimental Approaches to Hyaluronidase Structure Consolidation Due to Its Computational Interactions with Shortchain Glycosaminoglycan Ligands

Theoretical Grounding and Formation of Experimental Approaches to Hyaluronidase Structure Consolidation Due to Its Computational Interactions with Shortchain Glycosaminoglycan Ligands

Computational analysis of interaction between glycosaminoglycan ligands and 3D-model of hyaluronidase

Modification of Hyaluronidase Microenvironment: Innovatory Approaches for Development of Biocatalytic Medical Preparations

Contact Info

Product

Resources

About