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Characterization of a novel ?-conotoxin TxID from Conus textile that potently blocks rat ?3?4 nicotinic acetylcholine receptors.

ABSTRACT: The ?3?4 nAChRs are implicated in pain sensation in the PNS and addiction to nicotine in the CNS. We identified an ?-4/6-conotoxin (CTx) TxID from Conus textile. The new toxin consists of 15 amino acid residues with two disulfide bonds. TxID was synthesized using solid phase methods, and the synthetic peptide was functionally tested on nAChRs heterologously expressed in Xenopus laevis oocytes. TxID blocked rat ?3?4 nAChRs with a 12.5 nM IC50, which places it among the most potent ?3?4 nAChR antagonists. TxID also blocked the closely related ?6/?3?4 with a 94 nM IC50 but showed little activity on other nAChR subtypes. NMR analysis showed that two major structural isomers exist in solution, one of which adopts a regular ?-CTx fold but with different surface charge distribution to other 4/6 family members. ?-CTx TxID is a novel tool with which to probe the structure and function of ?3?4 nAChRs.

SUBMITTER: Luo S 

PROVIDER: S-EPMC4033315 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature

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Characterization of a novel α-conotoxin TxID from Conus textile that potently blocks rat α3β4 nicotinic acetylcholine receptors.

Luo Sulan S   Zhangsun Dongting D   Zhu Xiaopeng X   Wu Yong Y   Hu Yuanyan Y   Christensen Sean S   Harvey Peta J PJ   Akcan Muharrem M   Craik David J DJ   McIntosh J Michael JM  

Journal of medicinal chemistry 20131122 23

The α3β4 nAChRs are implicated in pain sensation in the PNS and addiction to nicotine in the CNS. We identified an α-4/6-conotoxin (CTx) TxID from Conus textile. The new toxin consists of 15 amino acid residues with two disulfide bonds. TxID was synthesized using solid phase methods, and the synthetic peptide was functionally tested on nAChRs heterologously expressed in Xenopus laevis oocytes. TxID blocked rat α3β4 nAChRs with a 12.5 nM IC50, which places it among the most potent α3β4 nAChR anta  ...[more]

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