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., ...More

JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY, vol.31, no.6, pp.1498-1501, 2016 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 31 Issue: 6
  • Publication Date: 2016
  • Doi Number: 10.3109/14756366.2016.1149479
  • Journal Name: JOURNAL OF ENZYME INHIBITION AND MEDICINAL CHEMISTRY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.1498-1501
  • Keywords: Acetylcholinesterase, butyrylcholinesterase, carbonic anhydrase, isatin, Mannich bases, DNA TOPOISOMERASE-I, CORRESPONDING PIPERIDINOLS, BIOLOGICAL EVALUATION, MEDICINAL CHEMISTRY, JURKAT CELLS, DERIVATIVES, HYDROCHLORIDES, DIHYDROCHLORIDE, CYTOTOXICITY, DISCOVERY
  • Çukurova University Affiliated: No

Abstract

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.