Chimeric peptides combining regions of peptide E and beta-endorphin revealed distinct structural requirements for mu vs delta opioid receptor activation, guiding design of receptor-selective opioid analgesics.
Key findingChimeric peptides combining regions of peptide E and beta-endorphin revealed distinct structural requirements for mu vs delta opioid receptor activati
What the researchers found
Chimeric peptides combining regions of peptide E and beta-endorphin revealed distinct structural requirements for mu vs delta opioid receptor activation, guiding design of receptor-selective opioid analgesics.
Why it matters
Relevant for peptide research.
How the study worked
research study.
What this study cannot tell us
See abstract.
How to read the evidence
emerging evidence.
When this study was published
Published in 2010.
The bigger picture
Advances peptide research.
Questions still open
- Further research needed.
Common questions
What was studied?
What was found?
Read the original research
Structural and pharmacological characteristics of chimeric peptides derived from peptide E and beta-endorphin reveal the crucial role of the C-terminal YGGFL and YKKGE motifs in their analgesic properties.
Peptides, 31(5), 962-72
Citation
Condamine, Eric; Courchay, Karine; Rego, Jean-Claude Do; Leprince, Jérôme; Mayer, Catherine; Davoust, Daniel; Costentin, Jean; Vaudry, Hubert. (2010). Structural and pharmacological characteristics of chimeric peptides derived from peptide E and beta-endorphin reveal the crucial role of the C-terminal YGGFL and YKKGE motifs in their analgesic properties.. Peptides, 31(5), 962-72. https://doi.org/10.1016/j.peptides.2010.01.012