NMR studies of the interaction of alpha-bungarotoxin with a mimotope of the nicotinic acetylcholine receptor

摘要

A combinatorial library approach has been used to produce synthetic peptides mimicking the snake neurotoxin binding site of nicotinic receptors.Among all the tested sequences which can inhibit the binding of alpha-bungarotoxin,alpha-bgt,to both muscle and neuronal nicotinic receptors,a 14-mer,with the sequence HRYYESSLPWYPD,henceforth called p6.7,has been selected ensuring a toxin-binding affinity considerably higher than other peptides reproducing native receptor sequences.NMR studies on the structural characteristics of the complex between the peptide and alpha-bungarotoxin are reported here.