In Vitro Inhibition Effects of 2-Amino Thiazole Derivatives on Lactoperoxidase Enzyme Activity

Abstract

Lactoperoxidase (LPO E.C. 1.11.1.7) is a member of the peroxidase family and is an important glycoprotein containing heme group in its structure and showing the antimicrobial effect on disease causing microorganisms in the digestive system of newborn babies. Thiazoles are the simplest members of heterocyclic compounds containing nitrogen and sulfur atoms in their structure. Many active pharmaceutical substances such as vitamin B1, penicillin, and those obtained by synthesis, contain a thiazole ring. It is desirable to evaluate the biological activities of thiazole derivatives, such as antiprotozoal antibacterial, antifungal, antituberculosis, and anthelmintic, with emphasis on their potential medical applications. The aim of this study was to determine the in vitro inhibition profiles of 2-amino thiazole derivatives against bovine LPO enzyme. In this study it was determined that all amino thiazole derivatives inhibited the LPO enzyme competitively. When the results were compared with each other, the 2-Amino-4-(4-chlorophenyl) thiazole compound showed the best inhibition effect against LPO with the Ki value of 250±100 nM.