Ghichi_2026_Acta.Crystallogr.C.Struct.Chem__

In the present work, we report on the synthesis, characterization and biological evaluation of (E)-5-(benzyloxy)-2-{[(2,5-dimethoxyphenyl)imino]methyl}phenol Schiff base, C(22)H(21)NO(4) (BDIMPh). The compound was synthesized via the condensation reaction between 4-benzyloxy-2-hydroxybenzaldehyde and 2,4-dimethoxyaniline. It was characterized using (1)H, (13)C NMR and FT-IR spectroscopies, and its crystal structure was determined by single-crystal X-ray crystallography. BDIMPh crystallizes with two crystallographically independent molecules in the asymmetric unit. The structural model also includes the reported disorder features, which are discussed on the basis of the crystallographic refinement. The two molecules of BDMPh have the same E configuration about the C=N bond. In the crystal, the independent molecules are linked to their inversion-related molecule via C-H...O hydrogen bonds. Hirshfeld surface analysis and two-dimensional fingerprint plots were used to quantify the intermolecular contacts present in the crystal. Quantum theory of atoms in molecules (QTAIM) analysis was performed to characterize selected intra- and intermolecular interactions. The optimized geometry showed good agreement with the experimental X-ray crystal structure. The antioxidant activity of BDIMPh was evaluated using the DPPH and ABTS radical-scavenging assays. BDIMPh exhibited moderate radical-scavenging activity under the experimental conditions and showed higher IC(50) values than the reference antioxidants. The enzyme inhibitory activity of BDIMPh was investigated against acetylcholinesterase (AChE), glutathione S-transferase (GST), alpha-glucosidase and tyrosinase. BDIMPh exhibited measurable enzyme-dependent inhibitory activity against AChE, GST and alpha-glucosidase, whereas comparatively weak inhibition was observed against tyrosinase. The IC(50) values were 2.899 +/- 0.851 microM for AChE, 3.850 +/- 0.721 microM for GST and 3.284 +/- 0.738 microM for alpha-glucosidase. Compared with the corresponding reference inhibitors, BDIMPh showed a slightly higher IC(50) value than donepezil for AChE, a slightly lower IC(50) value than ethacrynic acid for GST and a higher IC(50) value than acarbose for alpha-glucosidase. These results indicate an enzyme-dependent inhibitory profile rather than uniformly superior activity relative to the reference inhibitors.