Alpha-conotoxin AuIB isomers exhibit distinct inhibitory mechanisms and differential sensitivity to stoichiometry of alpha3beta4 nicotinic acetylcholine receptors.

@article{Grishin2010AlphaconotoxinAI,
  title={Alpha-conotoxin AuIB isomers exhibit distinct inhibitory mechanisms and differential sensitivity to stoichiometry of alpha3beta4 nicotinic acetylcholine receptors.},
  author={Anton A. Grishin and Ching-I Anderson Wang and Markus Muttenthaler and Paul F Alewood and Richard J Lewis and David J Adams},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 29},
  pages={
          22254-63
        }
}
Non-native disulfide isomers of alpha-conotoxins are generally inactive although some unexpectedly demonstrate comparable or enhanced bioactivity. The actions of "globular" and "ribbon" isomers of alpha-conotoxin AuIB have been characterized on alpha3beta4 nicotinic acetylcholine receptors (nAChRs) heterologously expressed in Xenopus oocytes. Using two-electrode voltage clamp recording, we showed that the inhibitory efficacy of the ribbon isomer of AuIB is limited to approximately 50%. The… CONTINUE READING
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