Secondary Sulfonamides as Effective Lactoperoxidase Inhibitors

KÖKSAL Z., KALIN R., Camadan Y., Usanmaz H., Almaz Z., GÜLÇİN İ., ...Daha Fazla

MOLECULES, cilt.22, sa.6, 2017 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 22 Sayı: 6
  • Basım Tarihi: 2017
  • Doi Numarası: 10.3390/molecules22060793
  • Dergi Adı: MOLECULES
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Anahtar Kelimeler: lactoperoxidase, secondary sulfonamide, enzyme purification, enzyme inhibition, CARBONIC-ANHYDRASE ISOENZYMES, AFFINITY-CHROMATOGRAPHY, BOVINE-MILK, DERIVATIVES, SYSTEM, ENZYME, PURIFICATION, DOPAMINE, XII, IX
  • Atatürk Üniversitesi Adresli: Evet

Özet

Secondary sulfonamides (4a-8h) incorporating acetoxybenzamide, triacetoxybenzamide, hydroxybenzamide, and trihydroxybenzamide and possessing thiazole, pyrimidine, pyridine, isoxazole and thiadiazole groups were synthesized. Lactoperoxidase (LPO, E.C.1.11.1.7), as a natural antibacterial agent, is a peroxidase enzyme secreted from salivary, mammary, and other mucosal glands. In the present study, the in vitro inhibitory effects of some secondary sulfonamide derivatives (4a-8h) were examined against LPO. The obtained results reveal that secondary sulfonamide derivatives (4a-8h) are effective LPO inhibitors. The K-i values of secondary sulfonamide derivatives (4a-8h) were found in the range of 1.096 x 10(-3) to 1203.83 mu M against LPO. However, the most effective inhibition was found for N-(sulfathiazole)-3,4,5-triacetoxybenzamide (6a), with K-i values of 1.096 x 10(-3) +/- 0.471 x 10(-3) mu M as non-competitive inhibition.