Special issue devoted to contributions presented at the 13th Naples Workshop on Bioactive Peptides, June 7-10, 2012, Naples.
Special Issue Article
Antinociceptive profile of potent opioid peptide AM94, a fluorinated analogue of biphalin with non-hydrazine linker†
Article first published online: 8 NOV 2012
Copyright © 2012 European Peptide Society and John Wiley & Sons, Ltd.
Journal of Peptide Science
Special Issue: Special issue devoted to contributions presented at the 13th Naples Workshop on Bioactive Peptides, June 7–10, 2012, Naples
Volume 19, Issue 4, pages 233–239, April 2013
How to Cite
Mollica, A., Costante, R., Stefanucci, A., Pinnen, F., Lucente, G., Fidanza, S. and Pieretti, S. (2013), Antinociceptive profile of potent opioid peptide AM94, a fluorinated analogue of biphalin with non-hydrazine linker. J. Peptide Sci., 19: 233–239. doi: 10.1002/psc.2465
- Issue published online: 24 MAR 2013
- Article first published online: 8 NOV 2012
- Manuscript Accepted: 10 OCT 2012
- Manuscript Revised: 9 OCT 2012
- Manuscript Received: 18 JUL 2012
- formalin test;
- molecular modeling;
- tail flick test;
- variable-temperature 1H NMR
AM94 is a fluorinated analog of biphalin with non-hydrazine linker that has an in vitro affinity for μ-opioid and δ-opioid receptors tenfold higher than biphalin. Furthermore, in vivo evaluation in rats showed that AM94 has in hot plate test – after both intracerebroventricular and intravenous administrations – a greater and more durable efficacy than biphalin. Here, the antinociceptive profile of AM94 is further evaluated by following two different administration routes, intrathecal and subcutaneous, and two different animal species, rats and mice. The analgesic potency of AM94 is compared with that of both the parent peptide biphalin and morphine. Results show that in rats (tail flick test) and in mice (formalin test), AM94 has a higher and more durable analgesic effect than biphalin after intrathecal and subcutaneous administrations. Conformational properties of biphalin and AM94 were also investigated by variable-temperature 1H NMR and energy minimization. Copyright © 2012 European Peptide Society and John Wiley & Sons, Ltd.