title: Interactions of narcotics and their antagonists with human serum esterase. VIII: structure-activity relationships of benzomorphans.
abstract: N-alkylbenzomorphans follow the pattern established in our earlier papers for the interaction of opiates with human serum esterase: they have affinity for both the substrate-binding site of the enzyme and an allosteric site at which agonistic drugs accelerate enzyme action. Affinity for the substrate-binding site is a function of the hydrophobicity of the drug, while affinity to the allosteric site is increased by alkyl groups at N and at C--5 and decreased by a 2'-methoxyl group or by either a methyl or a hydroxyl group in the 9 beta position. The absolute D configuration (corresponding to that of natural morphine) appears to be more sensitive to factors modifying affinity. All but three of the benzomorphans studied are agonists; all agonists have lower affinity for the allosteric site than antagonists.
mesh_terms: D001575:Benzomorphans / Q000031:analogs & derivatives / Q000097:blood*; D001665:Binding Sites; D002091:Butyrylcholinesterase / Q000097:blood; D002802:Cholinesterases / Q000097:blood; D004950:Esterases / Q000097:blood*; D006801:Humans; D007700:Kinetics; D008968:Molecular Conformation; D009019:Morphinans / Q000097:blood*; D009292:Narcotic Antagonists / Q000097:blood*; D009294:Narcotics / Q000097:blood*; D011485:Protein Binding; D013329:Structure-Activity Relationship
chemical_list: D001575:Benzomorphans; D009019:Morphinans; D009292:Narcotic Antagonists; D009294:Narcotics; D004950:Esterases; D002091:Butyrylcholinesterase; D002802:Cholinesterases