Noszál B, Kassai-Tánczos R, Nyíri J, Nyéki O, Schõn I
Department of Inorganic and Analytical Chemistry, L. Eötvös University, Budapest, Hungary.
Int J Pept Protein Res. 1991 Aug;38(2):139-45. doi: 10.1111/j.1399-3011.1991.tb01421.x.
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.
对21种免疫调节型胸腺生成素类二肽、三肽和四肽的亚分子碱度进行了研究，并根据基团常数和部分微常数进行了表征。所有化合物均为H-精氨酸-赖氨酸-天冬氨酸-OH三肽的衍生物。碱性位点四个共价键内的修饰（酯化、酰化、C末端的缩短或添加、氨基酸交换）会导致质子化方案和质子结合位点的个体碱度发生显著变化。然而，组成氨基酸的构型变化不会导致非对映异构体的碱度有显著差异。
