Synthesis and functional studies of tuftsin analogs containing isopeptide bond

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In the present paper a new approach is reported, to increase the resistance of tuftsin toward enzymatic cleavage by the introduction of an isopeptide bond into the molecule. The tetrapeptides H-Lys(Thr)-Pro-Arg-OH and H-Lys(Ala)-Pro-Arg-OH, the pentapeptides H-Thr-Lys(Ala)-Pro-Arg-OH, H-Thr-Lys(Thr)-Pro-Arg-OH and H-Ala-Lys(Ala)-Pro-Arg-OH and their For- and Boc-protected derivatives were built up by stepwise elongation of the chain, using conventional solution-phase methods. Preliminary experiments confirmed that from the Lys residue in position 2 of tuftsin the α-peptide bond between the Thr and Lys is cleaved with a significantly higher rate by leucine aminopeptidase than the ε{lunate}-peptide bond. Several of the isopeptide derivatives increased to a higher extent the interleukin (IL-1) secretion by monocytes than tuftsin or [Ala 1 ]-tuftsin.

Original languageEnglish
Pages (from-to)405-415
Number of pages11
Issue number3
Publication statusPublished - Jan 1 1990



  • Enzyme resistance increase
  • IL-1 secretion stimulation
  • Isopeptide bond
  • Tuftsin analogs

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience

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