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

[ X ]

Tarih

2022

Dergi Başlığı

Dergi ISSN

Cilt Başlığı

Yayıncı

Taylor & Francis Inc

Erişim Hakkı

info:eu-repo/semantics/closedAccess

Özet

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

Açıklama

Anahtar Kelimeler

Lactoperoxidase, enzyme purification, antibiotics, kinetics, enzyme inhibition

Kaynak

Journal of Biomolecular Structure & Dynamics

WoS Q Değeri

Q2

Scopus Q Değeri

Q1

Cilt

40

Sayı

1

Künye