Acid-base properties of thymopoietin-type tri- and tetrapeptides and their derivatives.

The submolecular basicities of 21 immuno-modulating, thymopoietin-type di-, tri-, and tetrapeptides were studied and characterized in terms of group constants and partial microconstants. All compounds were derivatives of the H-Arg-Lys-Asp-OH tripeptide. Modifications within four covalent bonds of the basic site (esterification, acylation, curtailment or addition at C-terminal end, exchange of amino acids) cause significant changes in the scheme of protonation and in the individual basicity of proton binding sites. Configurational changes of the component amino acids, however, do not cause significantly different basicities in the diastereomers.