Alpha-Bungarotoxin (aBTX)

α-Bungarotoxin (α-BTX) is one of the bungarotoxins, components of the venom of the elapid snake Taiwanese banded krait (Bungarus multicinctus). It is a type of α-neurotoxin, a neurotoxic protein that is known to bind irreversibly and competitively to the nicotinic acetylcholine receptor found at the neuromuscular junction, causing paralysis, respiratory failure and death in the victim. It has also been shown to play an antagonistic role in the binding of the α7 nicotinic acetylcholine receptor in the brain, and as such has numerous applications in neuroscience research. α-Bungarotoxin is a 74 amino acid, 8 kDa α-neurotoxin with five disulfide bridges that binds as a competitive antagonist to nicotinic acetylcholine receptors (nAChRs). As with other snake venom α-neurotoxins, it has a three-finger fold tertiary structure, which is a four disulfide globular core from which emerge three loops (fingers) and a C-terminal tail.