Akademik Veri Yönetim Sistemi
Journal of Molecular Structure, cilt.1354, sa.1, ss.144929, 2026 (Hakemli Dergi)
Trypsin and urease are biologically significant enzymes associated with digestive and pathogenic processes and represent key biochemical targets for inflammatory, ulcerative, and bacterial diseases. Designing metal-based inhibitors to modulate their activity is a promising strategy in medicinal inorganic chemistry. In this study, novel copper(II) and nickel(II) Schiff base complexes, [Cu(L)(bpy)] (1), [Cu(L)(phen)] (2), and [Ni(L)(phen)] (3), where L is derived from 5-chlorosalicylaldehyde and methionine, were synthesized and comprehensively characterized by UV–Vis, FTIR, ESI-MS, CHN analysis, and X-ray diffraction. Electronic absorption and fluorescence spectroscopy revealed minor-groove DNA binding and static quenching interactions with trypsin and urease. Molecular docking supported these findings by predicting favourable binding energies and highlighting key π–π stacking and hydrogen-bonding interactions. Antioxidant and enzymatic inhibition assays further indicated that the complexes exhibit notable free-radical scavenging and moderate inhibitory activity toward both enzymes. Taken together, this study provides integrated experimental and computational insights into the binding mechanisms and structure–activity relationships of Cu(II) and Ni(II) Schiff base complexes, offering a biophysical framework and a preliminary basis for future biological and pharmacological evaluations.