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

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dc.authoridMaraman, Muhammet/0000-0002-0155-3390
dc.authoridKORKMAZ, Isil Nihan/0000-0003-4896-5226
dc.authoridUSANMAZ, HANDE/0000-0003-3851-9601
dc.authoridgerni, serpil/0000-0001-7699-1697
dc.authoridBAYRAK, SONGUL/0000-0001-6424-2760
dc.authoridGulcin, ilhami/0000-0001-5993-1668
dc.contributor.authorKalin, Ramazan
dc.contributor.authorKoksal, Zeynep
dc.contributor.authorBayrak, Songul
dc.contributor.authorGerni, Serpil
dc.contributor.authorOzyurek, Isil Nihan
dc.contributor.authorUsanmaz, Hande
dc.contributor.authorKaraman, Muhammet
dc.date.accessioned2025-03-23T19:35:14Z
dc.date.available2025-03-23T19:35:14Z
dc.date.issued2022
dc.departmentSinop Üniversitesi
dc.description.abstractAntibiotics 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
dc.identifier.doi10.1080/07391102.2020.1814416
dc.identifier.endpage410
dc.identifier.issn0739-1102
dc.identifier.issn1538-0254
dc.identifier.issue1
dc.identifier.pmid32856529
dc.identifier.scopus2-s2.0-85089892928
dc.identifier.scopusqualityQ1
dc.identifier.startpage401
dc.identifier.urihttps://doi.org/10.1080/07391102.2020.1814416
dc.identifier.urihttps://hdl.handle.net/11486/5821
dc.identifier.volume40
dc.identifier.wosWOS:000563787200001
dc.identifier.wosqualityQ2
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherTaylor & Francis Inc
dc.relation.ispartofJournal of Biomolecular Structure & Dynamics
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.snmzKA_WOS_20250323
dc.subjectLactoperoxidase
dc.subjectenzyme purification
dc.subjectantibiotics
dc.subjectkinetics
dc.subjectenzyme inhibition
dc.titleMolecular docking and inhibition profiles of some antibiotics on lactoperoxidase enzyme purified from bovine milk
dc.typeArticle

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