Abstract
A synthetic immunogen representing a complex of a conjugate of a macromolecular carrier (natural protein) and a hapten (morphine drug) covalently bound to poly(4-nitrophenyl acrylate) (PNPA) has been developed. The macromolecular carrier in the conjugate is a human serum protein (human gamma-globulin, HGG, or human serum albumin, HSA). The optimal design of the synthetic immunogen was developed. The epitope accessibility and specificity of the immunogen complexes were investigated by ELISA. It was established that antigenic determinants are not shielded upon binding to antibodies for complexes with the optimal (1: 10) ratio of the conjugate to the synthetic polymer. The accute toxicity of PNPA was estimated. The immunogenicity of synthetic complexes was studied in rat immunization models. An influence of the immunogen structure and vaccination dose on the ability to produce specific antibodies to morphine was found.
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