Abstract
A peptide corresponding to residues 26–41 of α-bungarotoxin, and closed by a disulfide bond between two cysteine residues at the amino and C terminal ends of the peptide, was synthesized and the monomeric form was purified. The peptide, which represents the exposed part of the long central loop of the toxin molecule, was examined for binding to acetylcholine receptor. The peptide was shown by radiometric titrations to bind radiolabeled receptor, and radiolabeled peptide was bound by receptor. The specificity of the binding was confirmed by inhibition with the parent toxin. A synthetic analog of the peptide in which Trp-28 was replaced by glycine had very little (10%) of the original activity. Succinylation of the amino groups of the peptide resulted in virtually complete (98%) loss of the binding activity. These results indicate that a shortened loop peptide corresponding to the region 26–41 of α-bungarotoxin exhibits binding activities mimicking those of the parent molecule. In this region, Trp-28, and one or both of Lys-26 and Lys-38, are essential contact residues in the binding to receptor.
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Abbreviations
- AChR:
-
acetylcholine receptor
- BTX:
-
α-bungarotoxin ofBungarus multicinctus
- LII:
-
the monomer of the synthetic loop peptide corresponding to residues 26–41 of BTX (Fig. 1)
- LII(G):
-
an analog of peptide LII in which Trp-28 is replaced by glycine
- Su LII:
-
a derivative of LII succinylated at Lys-26
- Lys-38:
-
and the N-terminal
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McDaniel, C.S., Manshouri, T. & Atassi, M.Z. A novel peptide mimicking the interaction of α-neurotoxins with acetylcholine receptor. J Protein Chem 6, 455–461 (1987). https://doi.org/10.1007/BF02343342
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DOI: https://doi.org/10.1007/BF02343342