Neural Network Modeling of AChE Inhibition by New Carbazole-Bearing Oxazolones


ÇAVAŞ L., Topcam G., GÜNDOĞDU HIZLIATEŞ C., ERGÜN M. Y.

INTERDISCIPLINARY SCIENCES-COMPUTATIONAL LIFE SCIENCES, vol.11, no.1, pp.95-107, 2019 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 11 Issue: 1
  • Publication Date: 2019
  • Doi Number: 10.1007/s12539-017-0245-4
  • Journal Name: INTERDISCIPLINARY SCIENCES-COMPUTATIONAL LIFE SCIENCES
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.95-107
  • Keywords: AchE inhibition, Alzheimer's disease, Artificial neural network, Carbazole-bearing oxazolones, Enzyme inhibition, Organic synthesis, LIPASE-CATALYZED SYNTHESIS, THERMAL INACTIVATION, PREDICTION, DESIGN, ACETYLCHOLINESTERASE, DERIVATIVES, KINETICS, OPTIMIZATION, RELEASE, ANN
  • Dokuz Eylül University Affiliated: Yes

Abstract

Acetylcholine esterase (AChE) is one of the targeted enzymes in the therapy of important neurodegenerative diseases such as Alzheimer's disease. Many studies on carbazole- and oxazolone-based compounds have been conducted in the last decade due to the importance of these compounds. New carbazole-bearing oxazolones were synthesized from several carbazole aldehydes and p-nitrobenzoyl glycine as AChE inhibitors by the Erlenmeyer reaction in the present study. The inhibitory effects of three carbazole-bearing oxazolone derivatives on AChE were studied in vitro and the experimental results were modeled using artificial neural network (ANN). The developed ANN provided sufficient correlation between several dependent systems, including enzyme inhibition. The inhibition data for AChE were modeled by a two-layered ANN architecture. High correlation coefficients were observed between the experimental and predicted ANN results. Synthesized carbazole-bearing oxazolone derivatives inhibited AChE under in vitro conditions, and further research involving in vivo studies is recommended. An ANN may be a useful alternative modeling approach for enzyme inhibition.