Article 2022 · 11 citations

Molecular docking and inhibition profiles of some antibiotics on lactoperoxidase enzyme purified from bovine milk

Kalin, Ramazan, Koksal, Zeynep, Bayrak, Songul, Gerni, Serpil, Ozyurek, Isil Nihan, Usanmaz, Hande, Karaman, Muhammet, Atasever, Ali, Ozdemir, Hasan, Gulcin, Ilhami

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 (K-i) values of cefazolin were found as 8.19 and 34.66 mu M, 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

Keywords

Lactoperoxidase enzyme purification antibiotics kinetics enzyme inhibition ANHYDRASE ISOENZYMES I CARBONIC-ANHYDRASE ANTIOXIDANT ACTIVITY ANTIRADICAL ACTIVITIES ANTIBACTERIAL SYSTEM VITRO ANTIOXIDANT CAFFEIC ACID L-ADRENALINE PURIFICATION DERIVATIVES

WoS Categories

Biochemistry & Molecular Biology Biophysics

Sustainable Development Goals

Good Health and Well-being

Citation

Journal: JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
Year: 2022
Volume: 40
Issue: 1
Pages: 401-410
ISSN: 0739-1102
eISSN: 1538-0254
DOI: 10.1080/07391102.2020.1814416
WoS UID: WOS:000563787200001

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