Abstract
Heats of dilution of aqueous solutions of the following di-and tripeptides were determined at 25°C over a wide concentration range: β-alanyl-glycine, β-alanyl-β-alanine, DL-α-alanyl-glycine, glycyl-DL-α-alanine, L-α-alanyl-Lα-alanine, DL-α-alanyl-DL-α-alanine, DL-α-alanyl-DL-valine, DL-α-alanyl-β-alanine, glycyl-γ-aminobutyric acid, glycyl-L-leucine and DL-α-alanyl-glycylglycine. The excess enthalpies Hex and partial molar relative enthalpies L2 were calculated and enthalpy coefficients of intermolecular interaction were analysed using the additivity principle of Savage and Wood. The concentration dependence of the enthalpic characteristics of peptide-peptide interactions is discussed based on of their hydrophobicity and hydrophilicity. The three-stage model of peptide association is described using enthalpic coefficients of intermolecular interactions.
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Kulikov, O.V., Zielenkiewicz, A., Zielenkiewicz, W. et al. Excess enthalpies of aqueous solutions of small peptides at 25°C. J Solution Chem 22, 59–75 (1993). https://doi.org/10.1007/BF00647055
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DOI: https://doi.org/10.1007/BF00647055