Abstract
The interaction of gallium maltolate (Ga(ma)3) with human serum transferrin has been investigated by means of UV–Vis spectroscopy and isothermal titration calorimetry. First, the values of the first and second associative stepwise binding constants of Ga(ma)3 to apotransferrin were estimated by use of a data analyzing method. The synergistic role of the carbonate anion in the formation of gallium-transferrin bonds was also investigated. Experimental results indicated that the extent of binding is maximum at physiological pH. Citrate ion and transferrin have a competitive behavior toward gallium binding. By use of the calorimetric results, the values of 23.44 and 8.99 kJ mol−1 were determined for the associative stepwise enthalpy changes. This represents the endothermic entropy-driven nature of the process.
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