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Structural, Thermal and BSA binding analysis of L-Tryptophan derived Mn(III)/Fe(III) complexes | Abstract
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Abstract

Structural, Thermal and BSA binding analysis of L-Tryptophan derived Mn(III)/Fe(III) complexes

Author(s): R. Biju Bennie, C. Joel, S. Daniel Abraham, S. Theodore David and S. Iyyam Pillai

A novel N2O2 type ligand has been synthesized from 9, 10- Phenanthrenequinone and L-tryptophan and complexed with Mn(III) and Fe(III) metal ions. The synthesized ligand and its complexes were characterized by various spectral techniques such as FT-IR, UV-visible, 13C NMR, EPR, EI-Mass, elemental analysis, magnetic susceptibility and molar conductivity measurements. The metal complexes exhibit octahedral geometry. The thermal studies of the complexes were also carried out. The interaction of these synthesized metal complexes with Bovine Serum Albumin (BSA) has been studied using emission and absorption techniques. The Stern-Volmer quenching constants (Ksv), number of binding sites (n) and binding energy are calculated. It has been found that the metal complexes could bind to the hydrophobic pocket of BSA in sub-domain IIA. The energy transfer between the BSA and complexes have been studied using FRET and the donor acceptor distance was found to be less than 8 nm. The interaction of these metal complexes with BSA has been further supported by molecular docking studies.