In vitro stability of some reduced peptide bond pseudopeptide analogues of dynorphin A

Jean Philippe Meyer, Terrence J. Gillespie, Sharon Hom, Victor J. Hruby, Thomas P. Davis

Research output: Contribution to journalArticle

18 Scopus citations

Abstract

Eight analogues of DYN A(1-11)-NH2 incorporating the nonhydrolyzable Ψ[CH2-NH] peptide bond surrogate were tested for their in vitro enzymatic stability in mouse brain homogenates. Results show that the Leu5-Arg6 and to a lesser extent the Arg7-Ile8 and Ile8-Arg9 peptide bonds are the more susceptible to enzymatic cleavage in the native peptide. (Leu5Ψ[CH2-NH]Arg6)DYN A(1-11)-NH2 exhibits an almost complete resistance to enzymatic cleavage with a half-life greater than 500 min in brain, compared to 42 min for the standard peptide, DYN A(1-11)-NH2.

Original languageEnglish (US)
Pages (from-to)1215-1219
Number of pages5
JournalPeptides
Volume16
Issue number7
DOIs
StatePublished - 1995

Keywords

  • Dynorphin A
  • Enzymatic stability
  • Enzymes
  • Ψ[CH-NH] reduced bond

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience

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