Thermophilic proteases and their potential in thrombolytic therapy: a review of current research
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Abstract
Thermophilic and thermotolerant proteases are of considerable interest for biotechnology and medicine due to their unique stability and catalytic activity at elevated temperatures. This review is devoted to the systematization and analysis of modern studies of the hydrolytic activity of thermophilic proteases with a special focus on their thrombolytic and fibrinolytic properties. Based on the analysis of literature data, the structural and functional features of thermophilic proteases, the mechanisms of their action on various protein substrates, including fibrin and other components of blood clots, are considered. The relationship between thermal stability, substrate specificity, and the effectiveness of proteases as potential thrombolytic agents is analyzed. A comparative analysis of thermophilic proteases of various origins is presented in terms of their enzymatic activity, the influence of environmental factors, and their effectiveness in dissolving blood clots in vitro and in vivo. The advantages of thermophilic proteases over traditional thrombolytic drugs are considered, including increased stability, resistance to inhibitors, and potentially reduced side effects. Modern studies on the modification of thermophilic proteases to improve their thrombolytic properties and increase the specificity of action are analyzed. The prospects and limitations of the use of thermophilic proteases in clinical practice for the treatment of thrombotic conditions are discussed, as well as directions for further research in this area.
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References
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