Bioanalysis of Dermorphin, an Opioid Peptide in Equine Urine: Benefit of the VIP-Heated ESI Technology for the Quantitative Analysis of Thermally Labile Molecules

Bioanalytical

Bioanalysis of Dermorphin, an Opioid Peptide in Equine Urine: Benefit of the VIP-Heated ESI Technology for the Quantitative Analysis of Thermally Labile Molecules

22 Dec, 2012

Published over 13 years ago. See the latest and most current information on Bioanalytical.

Maurizio Splendore, Chris Kellogg and Rohan Thakur
1 min read
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Dermorphin is an opioid hepta-peptide derived from the skin secretions of South American frogs (Phyllomedusa sauvagei)1. It is 30-to-40 times more potent an analgesic than morphine2 and is unique because it contains D-alanine, a property that makes it highly resistant to protease mediated degradation (Figure 1). While d-amino acid peptides are sought after for their low immunogenic response and in peptidomimetic drug design, it was dermorphin’s use in horse racing that catapulted this opioid peptide from obscurity into the headlines. The pain-killing properties of dermorphin were used to drive racehorse performance beyond normal physical limits often injuring the animal. As a result, dermorphin is now a Class I prohibited substance as decreed by the Association of Racing Commissioners International (RCI) Model Rules3.
 

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