Investigation of collagenase and elastase inhibitory potential of the novel coordination compound

Extracellular matrix (ECM) consist of laminin, collagen, elastin, fibroblasts, and glycosaminoglycans. Its main role maintain the integrity and strength of organs as well as acts as a primary barrier to prevent the spread of the tumor cells because is a major component of the cellular microenvironment. The degradation of ECM involves different types of matrix metalloproteases (MMPs) such as collagenase and elastase. MMPs play a central role in major stages of tumor progression so novel potential inhibitors should be developed to prevent their protease activities. Coordination complexes have been used in medicine for their therapeutic properties. In the present study, we aim to investigate in vitro inhibitory effect of [Ni(edbea)Ag3(CN)5] against to collagenase and elastase activities by spectrophotometrically. Inhibition constant (Ki) of these enzymes was obtained from drawn Lineweaver Burk graphs. The complex containing silver exhibited effectively inhibitory effects on collagenase and elastase. Ki constants against to collagenase and elastase was found as 16.73+1.07 µM and 42.81 ± 9.62 µM, respectively. The IC50 value of the novel compound against to these enzymes was 10.66 µM and 49.5 µM, respectively. Inhibition type of the compound was noncompetitive against to collagenase and elastase activity. In conclusion, it has been indicated that novel dicyanidogylene compound have in vitro inhibitory effect on collagenase and elastase. In the future, the inhibitory effect of the molecule on ECM-degrading enzymes can be investigated in cell cultures and animal experiments for beneficial effects and the result may lead to designing potent new inhibitors. 1