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JOURNAL OF MOLECULAR STRUCTURE, vol.1354, 2026 (SCI-Expanded, Scopus)
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 it-it 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.