In vitro stability of some reduced peptide bond pseudopeptide analogues of dynorphin A
| Autor: | Thomas P. Davis, Terrence J. Gillespie, Sharon Hom, Victor J. Hruby, J.-P. Meyer |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
chemistry.chemical_classification
Male endocrine system Physiology Stereochemistry Half-life Dynorphin A Brain Peptide Dynorphin Cleavage (embryo) Biochemistry Dynorphins In vitro Cellular and Molecular Neuroscience chemistry.chemical_compound Mice Endocrinology Enzyme chemistry Drug Stability Endopeptidases Peptide bond Animals Half-Life |
| Zdroj: | Peptides. 16(7) |
| ISSN: | 0196-9781 |
| Popis: | Eight analogues of DYN A(1-11)-NH2 incorporating the nonhydrolyzable psi [CH2-NH] peptide bond surrogate were tested for their in vitro enzymatic stability in mouse brain homogenates. Results show that the Leu(5)-Arg6 and to a lesser extent the Arg(7)-Ile8 and Ile(8)-Arg9 peptide bonds are the more susceptible to enzymatic cleavage in the native peptide. (Leu5 psi[CH(2)-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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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