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Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis
Published on: January 7, 2017
Study of Al3+ interaction with AMP, ADP and ATP in aqueous solution
Paola Cardiano1, Claudia Foti1, Fausta Giacobello1
1Dipartimento di Scienze Chimiche, Biologiche, Farmaceutiche ed Ambientali, Università di Messina, Viale F. Stagno d'Alcontres 31, 98166 Messina, Italy.
Abstract:
The interaction of Al3+ and nucleotide ligands, namely adenosine-5'-monophosphate, (AMP), adenosine-5'-diphosphate, (ADP), adenosine-5'-triphosphate, (ATP), has been studied in aqueous solution at T = 298.15 K and I = 0.15 mol L-1 in NaCl (only for Al3+-ATP system at I = 0.1 mol L-1). Formation constants and speciation models for the species formed are discussed on the basis of potentiometric results. The speciation models found for the three systems include ML and ML2 species in all the cases, and for Al3+-ADP and ATP systems, MLH, MLOH and ML2OH species as well. The formation constant value for ML species shows the trend, AMP < ADP < ATP. 1H NMR spectroscopy was also employed for the study of Al3+-ATP system. The 1H NMR results are in agreement with the speciation model obtained from analysis of potentiometric titration data, confirming the stabilities of the main species. Enthalpy change values were obtained by titration calorimetry; for the main Al3+-ATP species (at T = 298.15 K and I = 0.1 mol L-1 in NaCl), they resulted always higher than zero, as typical for hard-hard interactions. The dependence of formation constants on ionic strength over the range I = 0.1 to 1 mol L-1 in NaCl is also reported for Al3+-ATP system. The sequestering ability of the nucleotides under study towards Al3+ was also evaluated by the empirical parameter pL0.5.
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