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Biotinyl-estradiol derivatives in enzyme immunoassays: structural requirements for optimal antibody binding.
Journal article

Biotinyl-estradiol derivatives in enzyme immunoassays: structural requirements for optimal antibody binding.

  • 1990-05-01
Published in:
  • Journal of steroid biochemistry. - 1990
Antigen-Antibody Reactions
Biotin
Chemical Phenomena
Chemistry
Chromatography, High Pressure Liquid
Estradiol
Immunoenzyme Techniques
Structure-Activity Relationship
English The use of the avidin/biotin complex in immunoassays is well documented. No comprehensive studies, however, are available on the structural requirements of the linkage between biotin and small molecules to get an optimal antigen-antibody interaction. We have synthesized seven different biotinylated estradiol derivatives. They were evaluated in an antibody- and in an antigen-immobilized enzyme immunoassay system. All three derivatives lacking a spacer group were useless for use in immunoassays, demonstrating the importance of a long distance between the biotin- and estradiol-moiety. In addition, the chemical structure of the linkage at the site of attachment to the steroid skeleton is very important for the antibody recognition: it may either be rigid but identical to that one used in the immunogen (6-carboxymethyloxime), or must be structurally flexible as exemplified by a 6-amido-linkage. A rigid structure (hydrazone) different from that of the immunogen absolutely prevents antibody binding.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/669
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