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

B. Noszál, R. Kassai-Tanczos, J. Nyiri, O. Nyeki, I. Schon

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
Publication statusPublished - 1991

Fingerprint

splenotritin
RGH 0205
Alkalinity
Derivatives
Amino Acids
Acids
Acylation
Esterification
Thymopoietins
Protons
Covalent bonds
Protonation
Binding Sites

ASJC Scopus subject areas

  • Biochemistry

Cite this

Acid-base properties of thymopoietin-type tri- and tetrapeptides and their derivatives. / Noszál, B.; Kassai-Tanczos, R.; Nyiri, J.; Nyeki, O.; Schon, I.

In: International Journal of Peptide and Protein Research, Vol. 38, No. 2, 1991, p. 139-145.

Research output: Contribution to journalArticle

Noszál, B. ; Kassai-Tanczos, R. ; Nyiri, J. ; Nyeki, O. ; Schon, I. / Acid-base properties of thymopoietin-type tri- and tetrapeptides and their derivatives. In: International Journal of Peptide and Protein Research. 1991 ; Vol. 38, No. 2. pp. 139-145.
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