Experimental and theoretical corroboration of antimicrobial and anticancer activities of two pseudohalides induced structurally diverse Cd (II)-Salen complexes

Abstract

Two new cadmium (II) complexes, viz., [Cd4(L1)2(ƞ1-NCS)2(µ2-ƞ2:ƞ1-OAc)2] (C1) and [Cd4(L2)2(µ1,1-N3)4]n (C2) (H2L1= N, N’-ethylene bis(3-methoxysalicylaldimine), H2L2= N, N’-ethylene bis(3-ethoxysalicylaldimine) were impeccably synthesized and structurally characterized using various sophisticated analytical techniques including SCXRD. X-ray diffraction confirmed complexes possess Cd4 structural motifs with two distinctive geometrical arrangements displayed around the central Cd (II) ion. Supramolecular architecture and multi-dimensional polymer formation reunited through the utilization of all anionic forms of ligands taken after by bridging bolster of pseudo-halide ions. Supramolecular interactions are more easily discernible through Hirshfeld surfaces and fingerprint plots. Herein, we demonstrated the potential role of the as-synthesized complexes towards the antimicrobial and anticancer activity. To address the issue, compounds are tested for antibacterial and antifungal activities against the bacteria Staphylococcus aureus (ATCC 25923), Bacillus subtilis (ATCC 6635), Pseudomonas aeruginosa (ATCC 27853), Escherichia coli (ATCC 25922), and fungal Candida albicans (ATCC 10231). The antimicrobial screening revealed that C1-C2 demonstrated higher action over ligands (L1-L2), thus, simply signifies the endowment of the compound's structural environment on these biological movements. Further, compounds anticancer activity was determined against A549 (Human lung carcinoma) and Panc-1 (Human pancreatic) lines using MTT assay. Molecular docking was performed to correlate the experimental binding results between complexes and the targeted proteins responsible for bacterial or cancerous features. Herewith, E. coli enzyme MurB (PDB ID: 2q85), B. subtilis SMC head domain (PDB ID: 5h67), cyclin-dependent kinase 2-associated protein 1 (PDB ID: 2kw6), and Epidermal Growth Factor Receptor (EGFR) tyrosine kinase domain (PDB ID: 1m17) have been selected to identify the true binding modes and docking poses, which are responsible for this superior biological activity. Subsequently, the current research puts in an exertion to crack a new Cd (II)-mediated complex as an antibacterial and anticancer drug which may demonstrate to be a moo fetched pharmaceutical.