Abstract
The group of synthetic low-molecular peptides exhibiting profound analgesic activity was developed by modifying the salmon calcitonin molecule fragment sCT(16-21), which retains the previously reported analgesic activity of the full-sized molecule. The mechanism of analgesic action of these synthetic oligopeptides has been investigated and their analgesic effect was compared with analgesic activity of ketorolac tromethamine, one of the strongest non-steroidal anti-inflammatory drug painkiller. It was demonstrated that the analgesic effect of the developed synthetic oligopeptides was associated with the specific binding of the clathrin heavy chain. It is postulated that inhibition of clathrin-mediated endocytosis of pain receptors in the postsynaptic vesicular cycle causes is more efficient analgesia than inhibition of those receptors on plasma membranes that may allow to replace opioid and non-steroidal anti-inflammatory drug’s analgesics with a much less toxic low-molecular synthetic peptides with non-narcotic type of analgesia.