Specificity of Rabbit Antibodies Elicited by Related Synthetic Peptides

• Published in: Zeitschrift für Naturforschung C. A journal of biosciences Vol. 41; no. 5; pp. 613 - 617
• Main Authors: Chersi, Alberto, Houghten, Richard A., Chillemi, Francesco, Zito, Romano, Centis, Dora
• Format: Journal Article
• Language: English
• Published: Germany Verlag der Zeitschrift für Naturforschung 01-06-1986
• Subjects: Amino Acid Sequence; Animals; Antibodies; Antigen-Antibody Complex; Peptide Fragments - immunology; Peptides - chemical synthesis; Peptides - immunology; Rabbit Antipeptide Antibodies; Rabbits - immunology; Structure-Activity Relationship; Synthetic Peptides
• ISSN: 0939-5075; 1865-7125
• DOI: 10.1515/znc-1986-5-620

Three 17-residue peptides, presenting from 65% to 70% sequence homology, and one endecapeptide, with no apparent homology with the first three, were chemically synthesized and investigated in their ability to elicit rabbit antipeptide antibodies.
The complex crossreactivities of the antisera were investigated by testing the binding of the antibodies to the intact peptides, to their enzymatic fragments, and by the use of specific immunoadsorbents.
Antipeptide antibodies may or may not crossreact with related “parent” peptides, this depending upon number, distribution, and localization of amino acid differences in low or high antigenicity regions of the immunogen.
Related peptides may elicit antibodies that crossreact almost completely, and therefore not specific for one or the other “parent” peptide. Those the selective recognition of closely related structures.