Journal of Biomolecular Structure and Dynamics · 2022 · 23 citations · 45 references
Life SciencesBiochemistryChemistryAnalytical ChemistryBiophysical ChemistryStructure-activity RelationshipsCoordination ChemistryLigand BindingMolecular DockingProtein-ligand BindingProtein-ligand DockingProtein-ligand InteractionsBovine Serum AlbuminLigand Binding AffinityMolecular Docking AnalysisProtein-ligand Complex AnalysisProtein-ligand Complex ModelingProtein-ligand ComplexesSpectroscopic CharacterizationVoltammetry
In this report, synthesis, characterization, biological and molecular modeling studies of Nophen Schiff base [N,N-bis(2-hydroxy-1-naphthaldehyde)-o-phenylenediamine] and Co(II)-Nophen complex have been furnished. BSA binding affinities of the ligand and Co(II)-Nophen complex have been appraised by UV-visible, fluorescence and cyclic voltammetric techniques. Spectroscopic measurements indicate strong binding of the complex with BSA protein through static quenching mechanism with binding constant in the order of 104 M−1. The negative shift of the peak potential in cyclic voltammetry suggested an electrostatic interaction. Molecular docking analysis reveals significant binding affinity (-6.3 kcal/mol) of the complex towards BSA protein. It is amazing that the in vitro cytotoxicity of Co(II)-Nophen complex against A549 cell lines (Human lung carcinoma cells) has remarkable potentials with 29 ± 1.2 µM as IC50 value. Comparing the biological activity towards microorganisms, Co(II)-Nophen complex show substantial response than the Nophen ligand.Communicated by Ramaswamy H. Sarma
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Nan Li, Ying Ma, Cheng Yang et al. · Biophysical Chemistry · 2005 · 256 citations
Pharmacy, Biophysics, Pharmacology +14
Mani Ganeshpandian, Loganathan Rangasamy, Eringathodi Suresh et al. · Dalton Transactions · 2013 · 198 citations