Epitope analysis: biotinylated short peptides as inhibitors of anti-peptide antibody

Epitope analysis: biotinylated short peptides as inhibitors of anti-peptide antibody

The interaction of anti-melittin antisera with melittin-coated ELISA plates could be inhibited by biotinylated peptides of the C terminal epitope which is one of three defined antigenic sites on the hexacosapeptide melittin. Non-biotinylated short peptides and peptide derivatives were inactive. It i...

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Veröffentlicht in:Journal of immunological methods 1989-12, Vol.125 (1), p.143-146
Hauptverfasser: Von Grünigen, R., Schneider, C.H.
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acid Sequence
Bee Venoms - immunology
Binding, Competitive
Biological and medical sciences
Biotin
Biotinylation
Epitope analysis
Epitopes
Fundamental and applied biological sciences. Psychology
Fundamental immunology
Melitten - immunology
Melittin
Molecular immunology
Molecular Sequence Data
Peptide inhibitor
Peptides - immunology
Structure-Activity Relationship
Techniques
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Zusammenfassung:The interaction of anti-melittin antisera with melittin-coated ELISA plates could be inhibited by biotinylated peptides of the C terminal epitope which is one of three defined antigenic sites on the hexacosapeptide melittin. Non-biotinylated short peptides and peptide derivatives were inactive. It is suggested that biotinylation of epitopic peptides enhances their inhibitory properties in a methodologically useful way.
ISSN:0022-1759
1872-7905
DOI:10.1016/0022-1759(89)90087-2