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Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII
Published on: August 31, 2018
Spectroscopic and molecular docking studies on the interaction of human serum albumin with copper(II) complexes
Bhargab Guhathakurta1, Ankur Bikash Pradhan1, Suman Das1
1Department of Chemistry, Jadavpur University, Kolkata, 700032, India.
Abstract:
Two osazone based ligands, butane-2,3-dione bis(2'-pyridylhydrazone) (BDBPH) and hexane-3,4-dione bis(2'-pyridylhydrazone) (HDBPH), were synthesized out of the 2:1M Schiff base condensation of 2-hydrazino pyridine respectively with 2,3-butanedione and 3,4-hexanedione. The X-ray crystal structures of both the ligands have been determined. The copper(II) complex of HDBPH has also been synthesized and structurally characterized. HDBPH and its copper(II) complex have thoroughly been characterized through various spectroscopic and analytical techniques. The X-ray crystal structure of the copper complex of HDBPH shows that it is a monomeric Cu(II) complex having 'N4O2' co-ordination chromophore. Interaction of human serum albumin (HSA) with these ligands and their monomeric copper(II) complexes have been studied by various spectroscopic means. The experimental findings show that the ligands as well as their copper complexes are good HSA binders. Molecular docking investigations have also been done to unravel the mode of binding of the species with HSA.
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