Immunologic approaches to the inhibition of renin and the adrenergic system.
It is uncommon for the small organic compounds used as drugs to possess unique target specificity. Thus, receptor antagonists as well as compounds that inhibit enzymes interact more widely than with their intended targets, actions that at times defeat the selectivity desired in their design. The antibody combining site, because it is a size larger than most drugs, has the capacity for a large number of interatomic contacts with its ligands, which provides the physical basis for increased selectivity and affinity. Two examples are described in applications where highly selective drugs are not available, the inhibition of the enzyme renin and the blockade of the beta 1-adrenergic receptor. Antibody specificity is achieved in the first instance by purifying the immunogen renin. In the second example, an antibody is generated in the absence of a purified beta receptor, by using a beta-blocking drug to generate an antibody that acts as a receptor model and the immunologic principle of anti-idiotypy to provide a second antibody that recognizes the receptor.
D000818:Animals; D000906:Antibodies; D000936:Antigen-Antibody Complex; D001667:Binding, Competitive; D001794:Blood Pressure; D004039:Diet, Sodium-Restricted; D004082:Dihydroalprenolol / Q000378:metabolism; D004285:Dogs; D007700:Kinetics; D011941:Receptors, Adrenergic / Q000276:immunology*; D011943:Receptors, Adrenergic, beta / Q000276:immunology* / Q000378:metabolism; D012083:Renin / Q000097:blood / Q000276:immunology*
D000906:Antibodies; D000936:Antigen-Antibody Complex; D011941:Receptors, Adrenergic; D011943:Receptors, Adrenergic, beta; D004082:Dihydroalprenolol; D012083:Renin