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Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII
Published on: August 31, 2018
Bovine serum albumin interaction, molecular docking, anticancer and antimicrobial activities of Co(II) Schiff base
J Jeevitha Rani1, A Mary Imelda Jayaseeli1, M Sankarganesh2
1Post Graduate and Research Center of Chemistry, Jayaraj Annapackiam College for Women (Autonomous), Affiliated to Mother Teresa Women's University, Kodaikanal, Periyakulam, Theni, Tamil Nadu, India.
Abstract:
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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