The examination of the effect of the firstly synthesized compounds like eperezolid on the enzyme activities of α-glucosidase and elastase

The α-glucosidase enzyme (E.C.3.2.1.20) on the small intestine epithelium is a hydrolase that converts starch and carbohydrates to glucose by reacting with α-1,4 bonds during digestion. The disorder of carbohydrate metabolism increases the blood glucose level and reveals the risk of diabetes mellitus by causing a rapid release of glucose. Diabetes mellitus is a chronic metabolic disease characterized by elevation of blood glucose that develops due to partial or total deficiency of insulin hormone. The inhibition of α-glucosidase activity is regarded as one of the most effective approaches to reduce postprandial glucose levels of blood. Therefore, α-glucosidase, enzyme inhibitors play an important role in the treatment of non-insulin dependent diabetes mellitus. Elastases, an important enzyme belonging to the chymotrypsin family of serine proteases, are responsible for the fragmentation of extracellular matrix proteins such as elastin and collagen, which are responsible for skin elasticity and strength. The increase of elastase enzyme leads to detoriation of extracellular matrix components, changes in the structure of elastic fibers and consequently it leads reduction of elastic properties of the skin and formation of wrinkle. In addition, the irregular and excessive release of elastase enzymes cause abnormal distortions in healthy tissues and this causes chronic wounds and inflammatory diseases. The development of elastase enzyme inhibitors due to these different effects is regarded as beneficial for protecting the skin elasticity and controling the elastase-associated diseases. Eperezolid is an oxazolidinone-derived agent which is a novel class of synthetic antimicrobials having bacteriostatic activity against a number of clinically important gram (+) bacteria. In this study, the examination of the effect of the firstly synthesized compounds like eperezolid on the enzyme activities of α-glucosidase and elastase. α-Glucosidase inhibition activity was determined by Khan et al., and elastase inhibition activity was determined by Moon et al. according to their methods spectrophotometrically.