Residues responsible for the selectivity of α-conotoxins for Ac-AChBP or nAChRs

Bo Lin, Shihua Xiang, Mengsen Li

Research output: Contribution to journalReview articlepeer-review

14 Scopus citations


Nicotinic acetylcholine receptors (nAChRs) are targets for developing new drugs to treat severe pain, nicotine addiction, Alzheimer disease, epilepsy, etc. α-Conotoxins are biologically and chemically diverse. With 12-19 residues and two disulfides, they can be specifically selected for different nAChRs. Acetylcholine-binding proteins from Aplysia californica (Ac-AChBP) are homologous to the ligand-binding domains of nAChRs and pharmacologically similar. X-ray structures of the α-conotoxin in complex with Ac-AChBP in addition to computer modeling have helped to determine the binding site of the important residues of α-conotoxin and its affinity for nAChR subtypes. Here, we present the various α-conotoxin residues that are selective for Ac-AChBP or nAChRs by comparing the structures of α-conotoxins in complex with Ac-AChBP and by modeling α-conotoxins in complex with nAChRs. The knowledge of these binding sites will assist in the discovery and design of more potent and selective α-conotoxins as drug leads.

Original languageEnglish (US)
Article number173
JournalMarine Drugs
Issue number10
StatePublished - Oct 1 2016


  • Ac-AChBP
  • Design
  • Model
  • Nachrs
  • X-ray structure
  • α-Conotoxins

ASJC Scopus subject areas

  • Drug Discovery


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