An insight into bactericidal, fungicidal, larvicidal and molecular docking studies of ruthenium(III) Schiff base complexes

• Published in: Chemical Data Collections Vol. 55; p. 101179
• Main Authors: Yesodharan, Sindhu, Sujatha, Bini Babu, Rajan, Pooja Parvathy, Susamma, Sujamol Mathunny, Janardhanan, Athira Chempakam, Kumar, Praveen, Raphael, Selwin Joseyphus, Kochukittan, Mohanan
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 01.02.2025
• Subjects: Amino acids; Antibacterial activity; Larvicidal; Molecular docking; Schiff base; Schiff base; Amino acids; Antibacterial activity; Larvicidal; Molecular docking
• ISSN: 2405-8300; 2405-8300
• DOI: 10.1016/j.cdc.2025.101179

This study presents the synthesis, molecular modelling, antibacterial, antifungal, larvicidal potential, and molecular docking studies of Ru(III) complexes derived from the Schiff bases, with six amino acids (glycine/α-alanine/phenylalanine/leucine/histidine/tryptophan) and 2‑hydroxy-1-naphthaldehyde. The chelation of the complexes has been explored using FT-IR, UV–Vis., and NMR spectral data. Furthermore, electrochemical, and magnetic studies favoured complexes' redox and coordination behaviour. The molar conductance values proved the non-electrolytic nature of the octahedral Ru(III) complexes. Comprehensive biological studies indicate that the Ru(III) complexes exhibit significant antibacterial activity against the gram-positive bacterium, Staphylococcus aureus. The complexes also exhibited enhanced larvicidal activity against Culex quinquefasciatus mosquito larvae. Correlation analysis of the larvicidal potentials has revealed the impact of the structural features on activity. The 3-D modelling of a few selected ligands and their complexes was also investigated. Molecular docking studies on the active site of different proteins also provided insights into the activities of the complexes. The results presented satisfactory -CDOCKER values for [Ru(III)-(NAA4)Cl(PPh3)2] and [Ru(III)-(NAA5)Cl(PPh3)2] suggesting a good binding affinity between the protein and the complexes. [Display omitted]