Abstract
Molar conductance (Λ) of ionizable side chains amino acids, lysine (Lys) and arginine (Arg) with dehydroascorbic acid (DHA) in water and in NaCl solutions was measured at temperatures range 298 K to 313 K. The limited molar conductance (Λo) and the constant of the ions association (KA) are calculated using the Shedlovsky techniques. The dynamic radius of the concerned ion (R) is calculated by used Stokes–Einstein relation. The heat of association, the Gibbs free energy, the change of entropy and activation energy (ΔHo/ kJ mol-1, ΔGo/ kJ mol-1, ΔSo/J K-1 mol-1, and ΔES/ kJ mol-1) respectively), also calculated. The data show increases the molar conductance with increase in temperature and decreasing in values at addition of DHA to Lys and Arg solutions. The association ions in NaCl solutions appear to increase in radius and decrease in diffusion coefficient relative to water solutions.ΔES, shows in most samples a positive value for the association and the values in NaCl solutions has lower relative to the water solutions. ΔGo is a trend to decrease with an increase in DHA concentration in water and NaCl solutions. The ion association is exothermic reaction relative to the negative value of ΔHo. The ΔSo andΔHo results, for Lys and Arg solutions, show decreasing in values at increase in DHA concentration in water and NaCl solutions. ΔGo (kJ mol-1), ΔSo (J K-1 mol-1), ΔHo (kJ mol-1), and ΔEs (kJ mol-1)
Highlights
Amino acids (AAs) are the main components of food
The activation energy of the association process in NaCl solutions has lower values relative to the same solutions in water and this refers to the increase in solubility of amino acids under study
hydrogen bonds (HB) have a tendency to associate the molecules in the solution so they have fewer random (ΔSo) as comparative to solution with no hydrogen bonding or lower, and this is seen at increase in dehydroascorbic acid (DHA) concentration in water and NaCl solutions
Summary
Amino acids (AAs) are the main components of food. AAs represent the principle building blocks required for biosynthesis of protein [1]. Many searches study the ion association between amino acids and different biological molecules [10,11,12], Since searching in ion association is key to knowledge the intermolecular interactions , structure-function relationships and structural biology. It is assist in drugs design that binds with targets selectively. This search reports the conductance measurements, the dynamic radiuses of the concerned ions, ion association constant and thermodynamic properties for DHA acid association with some ionizable side chains α-AAs (Lysine, Lys and Arginine, Arg) in water solution and sodium chloride solutions in the range 298–313 K of temperatures
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