Estimated membrane structure and receptor subtype selection of an opioid alkaloid-peptide hybrid.
Preferred conformation, orientation, and accumulation of dynorphin A-(1-8)-octapeptide, naltrexone, and N beta-(D-Leu-D-Arg-D-Arg-D-Leu-D-Phe)-naltrexamine (Lipkowsky et al., 1988) were estimated according to established procedures. Opioid binding site affinities and selectivities available from the literature were correlated with the estimated parameters of lipid membrane interaction. The results agreed with the molecular mechanism of opioid receptor subtype selection proposed earlier.
Schwyzer
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Department of Molecular Biology and Biophysics, Swiss Federal Institute of Technology (ETH), Zürich.
D000818:Animals; D001921:Brain / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism*; D004399:Dynorphins / Q000378:metabolism*; D006168:Guinea Pigs; D007700:Kinetics; D009271:Naltrexone / Q000031:analogs & derivatives* / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism*; D011957:Receptors, Opioid / Q000378:metabolism*; D013379:Substrate Specificity
D010446:Peptide Fragments; D011957:Receptors, Opioid; C059551:naltrexamine, N(beta)-(Leu-Arg-Arg-Leu-Phe)-; D009271:Naltrexone; D004399:Dynorphins; C026770:dynorphin (1-8)