Immunochemistry of scorpion toxins. Immunogenicity of peptide 19-28 a model of an accessible and relatively rigid region.
Peptide 19-28, a model of an antigenic region of Androctonus australis Hector toxin II, has a rigid alpha-helix structure in the native protein. It was used as immunogen either in the free form, or bound to bovine serum albumin (BSA) or linked to its synthesis support (macroporous polyacrylamide resin). Only the anti-(peptide-BSA) and the anti-(peptide-resin) antibodies recognized the native toxin. The use of short synthetic analogues of peptide 19-28 suggests a specificity difference in the two antipeptides. Anti-(peptide-BSA) recognizes probably two determinants localized at the C and N terminals of the peptide chain. Anti-(peptide-resin) preferentially recognizes the N-terminal extremity. Finally we showed that the alpha-helix region remains accessible to antipeptide 19-28 when the toxin is bound to its receptor.
D000595:Amino Acid Sequence; D000818:Animals; D000939:Epitopes / Q000032:analysis; D010446:Peptide Fragments / Q000276:immunology*; D011817:Rabbits; D011950:Receptors, Cholinergic / Q000378:metabolism; D012604:Scorpion Venoms / Q000276:immunology*; D015222:Sodium Channels; D013574:Synaptosomes / Q000378:metabolism
D000939:Epitopes; D010446:Peptide Fragments; D011950:Receptors, Cholinergic; D012604:Scorpion Venoms; D015222:Sodium Channels; C029574:scorpion toxin receptor