Molecular docking and inhibition profiles of some antibiotics on lactoperoxidase enzyme purified from bovine milk. Issue 1 (2nd January 2022)

• Record Type: Journal Article
• Authors: Kalin, Ramazan; Köksal, Zeynep; Bayrak, Songül; Gerni, Serpil; Ozyürek, Işıl Nihan; Usanmaz, Hande; Karaman, Muhammet; Atasever, Ali; Özdemir, Hasan; Gülçin, İlhami
• Is Part Of: Journal of biomolecular structure & dynamics. Volume 40:Issue 1(2022)
• Page Start: 401
• Page End: 410
• Publication Date: 2022-01-02
• Subjects: Lactoperoxidase -- enzyme purification -- antibiotics -- kinetics -- enzyme inhibition; Biomolecules -- Periodicals; Molecular structure -- Periodicals; Molecular Biology -- Periodicals; Biomechanics -- Periodicals; 572
• DOI: 10.1080/07391102.2020.1814416
• Languages: English
• ISSNs: 0739-1102

Abstract

Abstract: Antibiotics are generally used for human and veterinary applications to preserve and to control microbial diseases. Milk has a biologically significant enzyme known as lactoperoxidase (LPO) that is a member of peroxidase family. In metabolism, LPO has ability to catalyze the transformation of thiocyanate (SCN - ) to hypothiocyanite (OSCN - ) that is an antibacterial agent and the reaction occurs with hydrogen peroxide. In this work, LPO inhibition effects of some antibiotics including cefazolin, oxytetracycline, flunixin meglumine, cefuroxime, tylosin, vancomycin, chloramphenicol and lincomycin were tested. Among the antibiotics cefazolin was indicated the strongest inhibitory efficacy. The half maximal inhibitory concentration (IC50 ) and the inhibition constant (Ki ) values of cefazolin were found as 8.19 and 34.66 µM, respectively. It was shown competitive inhibition. 5-Methyl-1, 3, 4-thiadiazol-2-yl moiety activity plays a key role in the inhibition mechanism of cefazolin. Communicated by Ramaswamy H. Sarma