Inhibition of pancreatic elastase and by leaves extract and its constituents.

OBJECTIVE

Elastases are protease enzymes, which mainly hydrolyze proteins of the connective tissue, so they have a significant impact on human disease. is one of the species found in Indonesian mountains, and it has potential as an elastase inhibitor. The objective of this research was to examine the elastase inhibitor activity of leaves and to dock different ligands of its constituents against target protein of Porcine Pancreatic Elastase (PPE) receptor.

METHOD

Dried leaves powder of was extracted using Soxhlet apparatus with -hexane, ethyl acetate, and methanol. The extract was evaporated, and elastase inhibitor activity was determined using PPE with the quercetin used as control positive. Selected nine constituents of were evaluated on the docking behavior of elastase receptor using Protein-Ligand ANT System (PLANTS) computational software with PPE enzyme with Protein Data Bank (PDB) file 1BRU.

RESULT

The methanol extract showed significantly inhibited elastase with IC50 186.13 μg/mL, but ethyl acetate extract showed weak activity, and -hexane extract did not show any activity. Docking studies and binding free energy calculations and hydrogen bonding with some amino acids revealed that ellagic acid showed the least binding energy for the target enzyme.

CONCLUSION

This research has opened new insights into understanding that constituents of methanol extract are potential inhibitors against elastase, and suggested the active compound is ellagic acid.