Measuring the enthalpies of interaction between glycine, L-cysteine, glycylglycine, and sodium dodecyl sulfate in aqueous solutions

Abstract

Calorimetric measurements of enthalpies of solution Δ_solH^m for glycine, L-cysteine, and glycylglycine in aqueous solutions of sodium dodecyl sulfate (SDS) with concentrations of up to 0.05 mol kg^–1 are made. Standard enthalpy of solution Δ_solH⁰ and enthalpy of transfer Δ_trH⁰ of the dipeptide from water into mixed solvent are calculated. The calculated enthalpy coefficients of paired interactions of amino acids and dipeptide with SDS prove to be positive. Hydrophobic interactions between the biomolecules and SDS are found to have a major impact on the enthalpies of interaction in the three-component systems under study, within the indicated range of concentrations.