Opiorphin
Opiorphin is a peptide that was first isolated from human saliva. It is a relatively small molecule, consisting of only five amino acids, but it has been found to have potent analgesic properties.
Discovery[edit]
Opiorphin was discovered in 2006 by a team of researchers led by Catherine Rougeot at the Institut Pasteur in Paris, France. The team was investigating the analgesic properties of human saliva when they isolated the peptide.
Structure and Function[edit]
Opiorphin is a pentapeptide, meaning it is composed of five amino acids. These are glutamine, arginine, proline, arginine, and proline (QRPRL). The peptide is synthesized in the salivary glands and secreted into the saliva.
The primary function of opiorphin is to inhibit the breakdown of enkephalins, which are endogenous opioid peptides. It does this by inhibiting two enzymes, neutral endopeptidase (NEP) and aminopeptidase N (APN), which are responsible for degrading enkephalins. By preventing the breakdown of these peptides, opiorphin increases their concentration in the body, leading to increased analgesic effects.
Potential Therapeutic Uses[edit]
Due to its analgesic properties, opiorphin has potential for use in the treatment of pain. In animal studies, it has been found to be as effective as morphine in relieving pain, but without the side effects associated with opioid drugs. However, further research is needed to determine its safety and efficacy in humans.
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