DNA interaction, molecular dynamics simulation, molecular docking, biological, in vivo anti‐inflammatory and thermal studies of o‐hydroxyacetophenone and 2‐fluoroaniline Schiff base complexes

Series of transition metal complexes [Fe (HL)2Cl(H2O)](1), [Co (HL)2](2), [Ni (HL)2](3) and [Cu (HL)2](4) were derived on condensation of Schiff base ligand o‐hydroxyacetophenone with 2‐fluoroaniline in 1:1 ratio (HL) and characterized by spectral and analytical techniques. Based on the studies, complex 1 was found to be octahedral and complexes (2), (3) and (4) square planar. Coats–Redfern calculations suggest that all the complexes are non‐spontaneous and thermally stable. DNA binding studies revealed intercalation binding mode, while intrinsic binding constant (Kb) and Stern–Volmer quenching constant (Ksq) support high binding abilities. The nuclease activity using CT‐DNA was studied by gel electrophoresis. Docking studies were deduced using Accelry's Discovery Studio 2.1 program to understand binding affinities. The MD simulation, carried in order to analyse the stability of ligand and human topoisomerase I (PDB ID: 1T8I) complex for 100 ns using the Desmond 2020.1 from Schrödinger, LLC, revealed stable conformation of the ligand. In vivo, carrageenan induced inflammation studies in paw volume were carried out in rats, and results showed a higher rate of oedema inhibition for complex 4. Cytotoxicity and antimicrobial assay reveal that complex 4 exhibited higher cytotoxic and antimicrobial activity over other complexes and the ligand. The present paper involves metal complexes of Schiff base derived from o‐hydroxy‐acetophenone and 2‐fluoroaniline which were synthesized and characterized by sophisticated analytical techniques. DNA interaction studies revealed the intercalation of complexes to CT‐DNA. In vivo anti‐inflammatory, in vitro antimicrobial and cytotoxic studies (MTT assay) were performed for the complexes. Molecular dynamics simulation of the ligand with human topoisomerase I (PDB ID: 1T8I) revealed stable conformation of the ligand and docking studies of the complexes revealed binding affinities.