Anti-angiotensin antibodies cross-reactive with nonpeptide angiotensin antagonists as angiotensin receptor model
Anti-angiotensin II (Ang) antibodies could become important receptor mimicking tools if an antibody with binding properties identical to a particular Ang receptor could be generated. For this purpose, anti-Ang sera from mice were screened for antibodies with structure-affinity relationships similar or identical to a particular Ang receptor. Mice were immunized with BSA-coupled [Sar 1 ]Ang and the sera were screened in ELISA for crossreactivity with the Ang analogues saralasin, L158,809, EXP 3147, DuP 753, DuP 532, PD 123177, PD 123319 and the non-related compounds ACTH, naloxone, and CP 96,345. All sera had at least some cross-reactivity with saralasin and some also with L158,809, a potent non-peptide Ang antagonist, selective for the AT 1 site. One serum out of eight recognized most Ang analogues except the AT 2 selective PD 123177 and PD 123319. ELISA detection antigens were prepared by two different BSA conjugations: [Sar 1 ]Ang was N-terminally attached and [Sar 1 ,Lys 8 ]Ang was C-terminally attached. Against both detection antigens, the peptide antagonists saralasin and [Sar 1 ,Phe(Br 5 ) 8 ]Ang displaced in a sigmoidal manner the antibodies with an IC 50 -value of 0.4 mM. L158,809 and EXP 3147 displaced also in a parallel manner, suggesting an apparently homogenous population of binding sites. The selectivity profile of the serum has some resemblance to the AT 1 selectivity profile but the observed affinities are too low to suggest AT 1 receptor mimicry.
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