Inhibitory effects of isatin Mannich bases on carbonic anhydrases, acetylcholinesterase, and butyrylcholinesterase

Ozgun D. O., Yamali C., GÜL H. İ., Taslimi P., GÜLÇİN İ., YANIK T., ...Daha Fazla

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, cilt.31, sa.6, ss.1498-1501, 2016 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 31 Sayı: 6
  • Basım Tarihi: 2016
  • Doi Numarası: 10.3109/14756366.2016.1149479
  • Dergi Adı: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.1498-1501
  • Anahtar Kelimeler: Acetylcholinesterase, butyrylcholinesterase, carbonic anhydrase, isatin, Mannich bases, DNA TOPOISOMERASE-I, CORRESPONDING PIPERIDINOLS, BIOLOGICAL EVALUATION, MEDICINAL CHEMISTRY, JURKAT CELLS, DERIVATIVES, HYDROCHLORIDES, DIHYDROCHLORIDE, CYTOTOXICITY, DISCOVERY
  • Çukurova Üniversitesi Adresli: Hayır

Özet

The effects of isatin Mannich bases incorporating (1-[piperidin-1-yl (P1)/morpholin-4-yl (P2)/N-methylpiperazin-1-yl (P3)]methyl)-1H-indole-2,3-dione) moieties against human (h) carbonic anhydrase (CA, EC 4.2.1.1) isoenzymes hCA I and hCA II, acetylcholinesterase (AChE), and butyrylcholinesterase (BChE) enzymes were evaluated. P1-P3 demonstrated impressive inhibition profiles against AChE and BChE and also inhibited both CAs at nanomolar level. These inhibitory effects were more powerful in all cases than the reference compounds used for all these enzymes. This study suggests that isatin Mannich bases P1-P3 are good candidate compounds especially for the development of new cholinesterase inhibitors since they were 2.2-5.9 times better inhibitors than clinically used drug Tacrine.