Myeloperoxidase enzyme inhibition on favipiravir, levofloxacin, ceftriaxone, levodropropizine, budesonide, linezolid, caspofungin diacetate

Myeloperoxidase (MPO, EC 1.11.1.7) is an oxidoreductase and a major antimicrobial system enzyme in mammalian neutrophils. It is believed that human MPO and H2O2 produced by the active NADPH oxidase have antimicrobial functions in neutrophils and Kupffer cells. Due to the reactive species generated during the catalytic action of myeloperoxidase, which can react with normal biomolecules, the enzyme also contributes to cell and tissue damage in various inflammatory diseases. MPO is considered a factor in the etiology of inflammatory diseases, including atherosclerosis, disorders resulting from damage to the central nervous system, and certain types of tumors. The IC50 values for Favipiravir, Levofloxacin, Ceftriaxone, Levodropropizine, Budesonide, Linezolid, and Caspofungin diacetate on the myeloperoxidase enzyme were calculated as 53.31 µM, 53.31 µM, 36.48 µM, 43.32 µM, 43.32 µM, 49.51 µM, and 86.64 µM, respectively. The Ki values were determined as 0.30 nM, 0.73 nM, 0.63 nM, 0.14 nM, 540 nM, 740 nM, and 122 nM, respectively. These compounds exhibited competitive inhibition with the antioxidant enzyme for Favipiravir, Ceftriaxone, Levodropropizine, Budesonide, Linezolid, and Caspofungin diacetate, while Levofloxacin showed non-competitive inhibition. country.