The binding of chemically different psychotropic drugs to alpha 1-acid glycoprotein.
The clinical significance of the high-affinity binding of psychotropic compounds to alpha 1-acid glycoprotein (alpha 1-AGP) in human serum has not been established yet. However, this binding may be of considerable theoretical interest since glycoproteins play a prominent role in the structure of cell membranes. In order to elucidate the nature of the binding to alpha 1-AGP several typical psychotropic compounds (diazepam, haloperidol, imipramine, perazine, phenobarbital and phenytoin) were investigated by means of equilibrium dialysis. The results suggest that among the classical CNS-drugs only those with a tricyclic structure are bound to two binding sites. Possible reason for the widely differing binding of a series of drugs are discussed in terms of their different chemical structure.
D003975:Diazepam / Q000097:blood; D006220:Haloperidol / Q000097:blood; D006801:Humans; D007099:Imipramine / Q000097:blood; D007700:Kinetics; D009961:Orosomucoid / Q000097:blood*; D010464:Perazine / Q000097:blood; D010634:Phenobarbital / Q000097:blood; D010672:Phenytoin / Q000097:blood; D011485:Protein Binding; D011619:Psychotropic Drugs / Q000097:blood*; D013329:Structure-Activity Relationship
D009961:Orosomucoid; D011619:Psychotropic Drugs; D010672:Phenytoin; D010464:Perazine; D006220:Haloperidol; D007099:Imipramine; D003975:Diazepam; D010634:Phenobarbital