The synthesis, bioactivity and enzyme stability of D-Ala2, EPhe4, Leu5-enkephalins.
We have synthesized the first enkephalin analog containing a "cyclopropyl" phenylalanine (Phe) residue. The E-configuration of this residue is apparently responsible for its low activity in the MVD and GPI muscle assays. The enkephalin is very stable to cleavage by carboxypeptidase Y.
D000818:Animals; D001681:Biological Assay; D002268:Carboxypeptidases / Q000378:metabolism; D004743:Enkephalin, Leucine / Q000138:chemical synthesis* / Q000494:pharmacology; D006168:Guinea Pigs; D007082:Ileum / Q000502:physiology; D007202:Indicators and Reagents; D008297:Male; D051379:Mice; D009119:Muscle Contraction / Q000187:drug effects; D014649:Vas Deferens / Q000502:physiology
D007202:Indicators and Reagents; D004743:Enkephalin, Leucine; D002268:Carboxypeptidases; C022633:serine carboxypeptidase