Evaluation of acetylcholinesterase and carbonic anhydrase inhibition profiles of 1,2,3,4,6-pentasubstituted-4-hydroxy-cyclohexanes

KOÇYİĞİT Ü. M., TASLIMI P., GEZEGEN H., GÜLÇİN İ., Ceylan M.

JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY, cilt.31, sa.9, 2017 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 31 Sayı: 9
  • Basım Tarihi: 2017
  • Doi Numarası: 10.1002/jbt.21938
  • Dergi Adı: JOURNAL OF BIOCHEMICAL AND MOLECULAR TOXICOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Anahtar Kelimeler: acetylcholinesterase, carbonic anhydrase, domino reactions, enzyme inhibition pentasubstituted cyclohexanol, ISOENZYMES HCA I, ENZYME-ACTIVITY, SULFONAMIDE DERIVATIVES, ANTIOXIDANT ACTIVITY, MANNICH-BASES, ISOZYME-I, BUTYRYLCHOLINESTERASE, ESTERASE, XII, VITRO
  • Atatürk Üniversitesi Adresli: Evet

Özet

Carbonic anhydrase (CA; EC 4.2.1.1) is used for remedial purposes for several years, as there is significant focus on expanding more new activators (CAAs) and high affinity inhibitors. Alzheimers disease and other similar ailments such as dementia and vascular dementia with Lewy bodies reduce cholinergic activity in the important areas involved in cognition and memory. Prevalent drugs for the symptomatic therapy of dementia are significant in increasing the associated cholinergic deficiency by inhibiting acetylcholinesterase (AChE). These six-membered carbocycles showed nice inhibitory action against AChE and human carbonic anhydrase (hCA) II and I isoforms. The hCA I, II, and AChE were efficiently inhibited by these molecules, with K-i values in the range of 6.70-35.85nM for hCA I, 18.77-60.84nM for hCA II, and 0.74-4.60 for AChE, respectively.