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The capacity of antibodies to various synthetic peptides of α-bungarotoxin for binding peptides of the neurotoxin and recognizing the corresponding regions of the α-bungarotoxin molecule has been investigated. It has been established that individual conformational sections of the α-bungarotoxin molecule are specifically recognized by antibodies to synthetic epitopes of the neurotoxin.

This paper discusses literature reports over the last 12 years and the results of our own experimental investigations of the structures of the immune recognition regions of protein antigens — in particular presynaptic and postsynaptic neurotoxins from spider and snake venoms.

Using the method of solid-phase peptide synthesis, two peptides have been synthesized, one of which corresponds to the central ring structure of α-bungarotoxin (α-BTX), while the second has in position 28 a Gly residue in place of the Trp in the first peptide, and their interrelationship with antitoxin antibodies has been investigated. It has been shown that the amino acid residue Trp-28 of α-BTX, which is the contact residue in binding with the acetylcholine receptor, also participates directly in binding with the active centers of antibodies to α-BTX.