Unexpected Acylation Reaction Mechanism: Crystal Structure, Molecular Docking and AChE/BuChE Inhibition Analysis

AKGÜL F. G., Suhta A., Özşanli H., SANCAK K., Çoruh U.

Journal of Structural Chemistry, cilt.67, sa.1, ss.23-42, 2026 (SCI-Expanded, Scopus) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 67 Sayı: 1
  • Basım Tarihi: 2026
  • Doi Numarası: 10.1134/s002247662601004x
  • Dergi Adı: Journal of Structural Chemistry
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Chemical Abstracts Core, INSPEC
  • Sayfa Sayıları: ss.23-42
  • Anahtar Kelimeler: AChE/BuChE, acylation, aminothiazole, DFT, hydrazine carboxylate, molecular docking, thiazole, X-ray diffraction
  • Karadeniz Teknik Üniversitesi Adresli: Evet

Özet

Abstract: In this study, ethyl 2-(2-((ethoxycarbonyl)amino)thiazol-5-yl) acetate (4) was obtained by reacting ethyl 2-amino thiazol-4 acetate (1) and different hydrazine carboxylate derivatives (2) via an acylation route different from the synthesis plan. The spectra of the synthesized ethyl 2-(2-((ethoxycarbonyl)amino)thiazol-5-yl) acetate (4) were examined and its structure was determined. FTIR, 1H NMR, 13C NMR and Mass spectra were recorded, and structural analyses were completed by using these spectral data. Studies on the structure of compound 4 support its synthesis as a product of an acylation reaction. Crystal structure studies on compound 4, including structural X-ray study, theoretical DFT calculations, Hirshfeld surface analysis and molecular docking study that include inhibition of breast cancer protein (PDB ID: 4XO6) have been conducted for the first time. Inhibition studies of acetylcholinesterase, butyrylcholinesterase were performed to determine the inhibitory properties of the compound 4.