Synthesis and analgesic activity of human beta-endorphin.
The solid-phase synthesis of human beta-endorphin is described. A yield of 32% is achieved based on starting resin. The synthetic product behaves as a homogeneous peptide in partition chromatography, paper electrophoresis, thin-layer chromatography, disc electrophoresis, amino acid composition, and a tryptic map. The synthetic beta h-endorphin possesses antinociceptive properties as estimated by the tail-flick, hot-plate, and writhing tests in mice. When applied centrally, beta h-endorphin is 17-48 times more potent than morphine. It is 3.4 times more potent than morphine when injected intravenously. The analgesic responses are blocked by the specific opiate antagonist, naloxone.
D000595:Amino Acid Sequence; D000700:Analgesics / Q000138:chemical synthesis*; D000818:Animals; D008297:Male; D008722:Methods; D051379:Mice; D008813:Mice, Inbred ICR; D009020:Morphine / Q000494:pharmacology; D009270:Naloxone / Q000494:pharmacology; D010455:Peptides / Q000037:antagonists & inhibitors / Q000138:chemical synthesis* / Q000494:pharmacology; D011930:Reaction Time / Q000187:drug effects
D000700:Analgesics; D010455:Peptides; D009270:Naloxone; D009020:Morphine