COMPARATIVE MOLECULAR DOCKING ANALYSIS OF SELECTED AROMATIC COMPOUNDS WITH DISTINCT ENZYME SYSTEMS

Ünlü N., Özgen A.

VIII. International Agricultural, Biological & Life Science Conference, İstanbul, Türkiye, 06-09 September 2026, İstanbul, Türkiye, 6 - 09 Eylül 2026, ss.816, (Özet Bildiri)

  • Yayın Türü: Bildiri / Özet Bildiri
  • Basıldığı Şehir: İstanbul
  • Basıldığı Ülke: Türkiye
  • Sayfa Sayıları: ss.816
  • İstanbul Gelişim Üniversitesi Adresli: Evet

Özet

Aromatic amines and phenolic compounds are widely used in the cosmetic and chemical industries, particularly in hair dye formulations, and their interactions with enzymatic systems are relevant to biotransformation, contaminant removal and industrial bioprocesses. In this study, the binding tendencies of 3-aminophenol, 4-aminophenol, p-phenylenediamine, resorcinol and the toxicologically important aromatic amine 2-naphthylamine toward Cel7A cellobiohydrolase (PDB: 1EGN), cytochrome P450cam (PDB: 1GJM) and a fungal laccase (PDB: 3PPS) were investigated by molecular docking. Cel7A was selected to represent the potential interaction of aromatic compounds with enzymes involved in lignocellulosic processing, whereas P450cam and laccase represented heme- and copper-dependent oxidative biotransformation systems, respectively. The predicted binding energies of the 15 protein– ligand complexes ranged from −4.5 to −7.3 kcal/mol. 2-Naphthylamine generated the most negative docking scores for all three targets, with binding energies of −7.2, −7.3 and −6.8 kcal/mol for 1EGN, 1GJM and 3PPS, respectively. The remaining ligands produced closely clustered binding energies ranging from −4.5 to −5.5 kcal/mol. These findings indicate a distinct and consistent predicted binding tendency of 2-naphthylamine toward three microbial enzymes with different structural and catalytic properties. The results may provide preliminary data for further experimental investigations into the enzymatic biotransformation and removal of dye industry-related aromatic compounds and their potential interactions with industrially relevant enzymes.