Crataegus monogyna and Centella asiatica Extracts as Inhibitors of Cathepsin S

Abstract

Cathepsin cysteine proteases such as cathepsin S are responsible for the unfavorable and irreversible dysregulation of extracellular matrix (ECM) proteolysis found in cardiomyopathy, heart valve diseases and atherosclerosis. Cathepsin S plays a central role in ECM remodeling, which has been implicated in the development and progression of cardiovascular diseases. The current study aimed to evaluate the aqueous and ethanol extracts of the berries of Crataegus monogyna and the leaves of Centella asiatica for inhibition of cathepsin S activity using an in vitro fluorescent assay. Dried and ground berries of Crataegus monogyna and the dried and ground leaves of Centella asiatica were used to prepare the aqueous and organic extracts. A fluorometric enzyme assay was used to evaluate the inhibition of cathepsin S by the plant extracts. The aqueous extracts of Crataegus monogyna and Centella asiatica produced a maximum enzyme inhibition of 6% and 9.6% respectively, at a maximum of 200 μg/ml. The organic extract of Centella asiatica produced a maximum inhibition of 14%, occurring with the 100 μg/ml concentration. The ethanol extract of Crataegus monogyna produced a concentration-dependent inhibition of cathepsin S enzyme activity for all concentrations, with a maximum inhibition of 71.7% obtained with the highest concentration of 200 μg/ml. This demonstrates that the organic extract of Crataegus monogyna plays a crucial role in the inhibition of cathepsin S in vitro and could serve as a viable source for the isolation of cathepsin S inhibitors.