Biologische Abbaubarkeit von synthetischen verzweigten Polypeptiden mit Poly (L-lysin)-Rückgrat

Translated title of the contribution: Biodegradability of Synthetic Branched Polypeptide With Poly(L-Lysine) Backbone

Ferenc Hudecz, Sára Kutassi-Koávcs, Gábor Mezö, Mária Szekerke

Research output: Contribution to journalArticle

27 Citations (Scopus)


A detailed investigation is reported about the biodegradation of poly[Lys(DL-Alam)], m ˜ 3, (AK) the common inside area of a branched polypeptide model system developed by our group over the last decade. Enzymatic hydrolysis was carried out by the exopeptidase aminopeptidase M, or the endopeptidase trypsin, or their mixture. Ion-exchange column chromatography, paper electrophoresis and thinlayer chromatography were utilised to achieve separation of metabolites. Breakdown products were identified by the aid of synthetic oligopeptides representing the potential fragments (DL-Alam), DL-Ala2, Lys(DL-Alam), m = 1-3).The kinetics and the degree of enzymatic degradation were determined.The ratio of peptide/amino acid amounts in the hydrolysate was found to be 1.07 after 24 h treatment with aminopeptidase M, 3.0 with trypsin and 1.3 with aminopeptidase - trypsin mixture. The overall results indicated that the proteolysis of AK by an aminopeptidase M and trypsin mixture proceeds stepwise at multiple sites on the polypeptide chain. The degradation is significantly retarded as compared to that of μ- or U03FS-polylysine. A mechanism of degradation is suggested based on the experimental results.

Translated title of the contributionBiodegradability of Synthetic Branched Polypeptide With Poly(L-Lysine) Backbone
Original languageUndefined/Unknown
Pages (from-to)1019-1026
Number of pages8
JournalBiological Chemistry Hoppe-Seyler
Issue number2
Publication statusPublished - Jan 1 1989


  • Branched polypeptides
  • enzymatic hydrolysis
  • identification of metabolites
  • mechanism of degradation
  • synthesis of oligopeptides

ASJC Scopus subject areas

  • Biochemistry

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