Acid‐base properties of thymopoietin‐type tri‐ and tetrapeptides and their derivatives

BÉLA NOSZÁL, RÓZSA KASSAI‐TÁNCZOS, JUDIT NYÍRI, OLGA NYÉKI, ISTVÁN SCHÕN

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)139-145
Number of pages7
JournalInternational journal of peptide and protein research
Volume38
Issue number2
DOIs
Publication statusPublished - Aug 1991

Keywords

  • acid‐base equilibria
  • dissociation constants
  • microspeciation
  • submolecular basicity
  • thymopoietin‐type oligopeptides

ASJC Scopus subject areas

  • Biochemistry

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