Lactoperoxidase, an antimicrobial enzyme, is inhibited by some indazoles.


Journal

Drug and chemical toxicology
ISSN: 1525-6014
Titre abrégé: Drug Chem Toxicol
Pays: United States
ID NLM: 7801723

Informations de publication

Date de publication:
Jan 2020
Historique:
pubmed: 22 8 2018
medline: 2 10 2020
entrez: 22 8 2018
Statut: ppublish

Résumé

Lactoperoxidase (LPO) has bactericidal and bacteriostatic activity on various microorganisms and it creates a natural antimicrobial defense system. So, LPO is one of the essential enzyme in biological systems and the protection of the LPO activity is extremely important for the immune system. Because of these features, the protection of the activity of the LPO has vital importance for the health of the organisms. Also, LPO is used in various sectors from cosmetics industry to agriculture industry due to its broad antimicrobial properties. Therefore, the identification of inhibitors and activators of the LPO is becoming increasingly important. In present study we aimed to investigate the inhibitory effects of some indazoles [1H-indazole (1a), 4-Bromo-1H-indazole (2a), 6-Bromo-1H-indazole (3a), 7-Bromo-1H-indazole (4a), 4-chloro-1H-indazole (5a), 6-chloro-1H-indazole (6a), 7-chloro-1H-indazole (7a), 4-fluoro-1H-indazole (8a), 6-fluoro-1H-indazole (9a), 7-fluoro-1H-indazole (10a)] on bovine milk LPO. Indazole derivatives are heterocyclic organic molecules with a wide range of biological activity. For this aim, bovine milk LPO was purified using Sepharose-4B-l-tyrosine-5-amino-2-methyl benzenesulfonamide affinity chromatography method. Then, the potential inhibitory effects of indazoles on LPO activity were investigated.

Identifiants

pubmed: 30126312
doi: 10.1080/01480545.2018.1488861
doi:

Substances chimiques

Enzyme Inhibitors 0
Indazoles 0
Lactoperoxidase EC 1.11.1.-

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

22-26

Auteurs

Zeynep Köksal (Z)

Faculty of Engineering and Natural Sciences, Department of Chemistry, Istanbul Medeniyet University, Istanbul, Turkey.

Zuhal Alim (Z)

Faculty of Science and Arts, Department of Chemistry, Ahi Evran University, Kırşehir, Turkey.

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Classifications MeSH