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Biophysical analysis of interaction between curcumin and alpha-2-macroglobulin

Ali, Syed Saqib, Zia, Mohammad Khalid, Siddiqui, Tooba, Ahsan, Haseeb, Khan, Fahim Halim
International journal of biological macromolecules 2019 v.128 pp. 385-390
Fourier transform infrared spectroscopy, Gibbs free energy, active sites, anti-inflammatory activity, antioxidant activity, binding sites, body fluids, calorimetry, curcumin, enthalpy, entropy, glycoproteins, heat production, proteinases, spices, titration, vertebrates, India
Alpha-2-macroglobulin (α2M) is large glycoprotein present in the body fluids of vertebrates. It is an antiproteinase that inhibits a broad spectrum of proteases without the direct blockage of the protease active site. Curcumin, a yellow spice commonly used in India and several Asian countries, is reported to have anti-tumor and anti-inflammatory effects because of its antioxidant properties. In the present study, we have explored the interaction of curcumin with α2M using various technique such as antiproteinase activity assay, spectroscopy. Changes in the secondary structure of α2M following interaction with curcumin was investigated by CD and FT-IR spectroscopy. Thermodynamics of curcumin-α2M binding were also analyzed by isothermal titration calorimetry to identify the number of binding sites, changes in enthalpy, entropy and Gibbs free energy changes for this interaction. Thermodynamics parameters reveal that the binding is exothermic in nature. Our results suggest that the binding of curcumin with α2M induces a conformational change in the native form of protein that compromises its anti-proteinase activity. This exothermic and spontaneous interaction leads to alteration in the β-sheet content of the protein leading to subtle changes in conformational status of the protein leading possibly to loss in the antiproteinase potential of the inhibitor.