Discovery of Potent Carbonic Anhydrase and Acetylcholinesterase Inhibitors: 2-Aminoindan beta-Lactam Derivatives

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GENÇ H., KALIN R., KÖKSAL Z., Sadeghian N., KOÇYİĞİT Ü. M., ZENGİN M., ...Daha Fazla

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, cilt.17, sa.10, 2016 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 17 Sayı: 10
  • Basım Tarihi: 2016
  • Doi Numarası: 10.3390/ijms17101736
  • Dergi Adı: INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Anahtar Kelimeler: carbonic anhydrase, acetylcholinesterase, beta-lactam, 2-azetidinone, enzyme inhibition, enzyme purification, ERYTHROCYTE ISOZYMES I, ISOENZYMES HCA I, ENZYME-ACTIVITY, SULFONAMIDE DERIVATIVES, ESTERASE INHIBITORS, PHENOLIC-COMPOUNDS, PURIFICATION, VITRO, SULFAMIDES, LACTOPEROXIDASE
  • Sivas Cumhuriyet Üniversitesi Adresli: Evet

Özet

beta-Lactams are pharmacologically important compounds because of their various biological uses, including antibiotic and so on. beta-Lactams were synthesized from benzylidene-inden derivatives and acetoxyacetyl chloride. The inhibitory effect of these compounds was examined for human carbonic anhydrase I and II (hCA I, and II) and acetylcholinesterase (AChE). The results reveal that beta-lactams are inhibitors of hCA I, II and AChE. The Ki values of beta-lactams (2a-k) were 0.44-6.29 nM against hCA I, 0.93-8.34 nM against hCA II, and 0.25-1.13 nM against AChE. Our findings indicate that beta-lactams (2a-k) inhibit both carbonic anhydrases (CA) isoenzymes and AChE at low nanomolar concentrations.