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Alpha-Bungarotoxin

Alpha-Bungarotoxin (α-BGT) is a nicotinic cholinergic antagonist that is found within the venom of Bungarus multicinctus, a South-asian snake commonly known as kraits. α-BGT is known to bind irreversibly to the acetylcholine receptor found at the neuromuscular junction, causing respiratory failure, paralysis, and death, as well as play an antagonstic role in binding the α7 nicotinic acetylcholine receptor in the brain.

Structure

General Structure

Functions

α7 nicotinic acetylcholine receptor binding

Reponse to sensory stimuli and seizure genesis has been linked to nicotinic mechanisms^[1].

Seizure genesisa nd habituation of responseto sensorys timuli have been linked to nicotinic mechanisms (Marks et al., 1989; Luntz-Leybman et al., 1992). These functions are closely associated with the CA3 field (Schwartzkroin, 1986; Bickford- Wimer et al., 1990). Nicotinic responsesa re mediated by two major classeso f receptors, ganglionic type and neuromuscular type. Pharmacological analysis of both seizure genesis and habituation in rat brain implicates mediation by a neuromuscular type (Miner and Collins, 1989; Luntz-Leybman et al., 1992). These data are supported by the prominent binding of the neuromuscular- type antagonist oc-bungarotoxin (a-BT) in the CA3 field of the hippocampus (Hunt and Schmidt, 1978; Segal et al., 1978; Clarke et al., 1985

neuromuscular acetylcholine receptor binding

References

1. ↑ a-Bungarotoxin Binding to Hippocampal Interneurons: lmmunocytochemical Characterization and Effects on Growth Factor Expression