Interaction of copper (II) complexes by bovine serum albumin: spectroscopic and calorimetric insights

Journal of Biomolecular Structure & Dynamics
Namrata SinghNand Kishore


Serum albumins being the most abundant proteins in the blood and cerebrospinal fluid are significant carriers of essential transition metal ions in the human body. Studies of copper (II) complexes have gained attention because of their potential applications in synthetic, biological, and industrial processes. Study of binding interactions of such bioinorganic complexes with serum albumins improves our understanding of biomolecular recognition process essential for rational drug design. In the present investigation, we have applied quantitative approach to explore interactions of novel synthesized copper (II) complexes viz. [Cu(L1)(L2)ClO4] (complex I), [Cu(L2)(L3)]ClO4] (complex II) and [Cu(L4)2(H2O)2] (complex III) with bovine serum albumin (BSA) to evaluate their binding characteristics, site and mode of interaction. The fluorescence quenching of BSA initiated by complexation has been observed to be static in nature. The binding interactions are endothermic driven by entropic factors as confirmed by high sensitivity isothermal titration calorimetry. Changes in secondary and tertiary structure of protein have been studied by circular dichroism and significant reduction in α-helical content of BSA was observed upon binding. Sit...Continue Reading


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Methods Mentioned

isothermal titration
circular dichroism
fluorescence spectroscopy
fluorescence titration
Differential Scanning Calorimetery

Software Mentioned


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