Acid‐base properties and microspeciation of six angiotensin‐type octapeptides

OLGA NYÉKI, ERZSÉBET OSZTAS, BÉLA NOSZÁL, KÁLMÁN BURGER

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5 Citations (Scopus)

Abstract

The acid‐base chemistry of six angiotensin II analogues (A 11) was analyzed by determining two types of terms. Macroconstants were used to characterize the molecular proton‐binding and dissociating ability of the octapeptides, and group constants to quantitate the submolecular basicity of each individual protona‐tion site of the derivatives. The group constant values indicated that some sites (Arg‐guanidino, Tyrphenolate, C‐terminal carboxylate) were of similar basicity in the different analogues, while others (Hisimidazole, N‐terminal amino) were significantly different. The group constant values are interpreted by taking into consideration the intramolecular effects of the adjoining moieties and are used for microspeciation.

Original languageEnglish
Pages (from-to)424-427
Number of pages4
JournalInternational journal of peptide and protein research
Volume35
Issue number5
DOIs
Publication statusPublished - May 1990

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Keywords

  • acid‐base equilibria
  • angiotensin II
  • angiotensin II antagonists
  • dissociation constants
  • microspeciation
  • submolecular basicity

ASJC Scopus subject areas

  • Biochemistry

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