It is a type of α-neurotoxin, a neurotoxic protein that is known to bind competitively and in a relatively irreversible manner to the nicotinic acetylcholine receptor found at the neuromuscular junction, causing paralysis, respiratory failure, and death in the victim.

[citation needed] These neurotoxins primarily affect the nervous system, blocking the nerve impulse transmission,[4] leading to paralysis and potentially death if untreated.

It was characterized by its distinctive black-and-white banded pattern along its body, with a maximum length of 1.85 m. This very venomous species is found in central and southern China and Southeast Asia.

[6][7][8] In South and Southeast Asia, envenomation from the many-banded krait bite is a common and life-threatening medical condition when not promptly treated.

[12] In addition, the severity of the paralysis ranges from mild to life-threatening depending on the degree of envenomination, its composition and the early therapeutic intervention.

On the other hand, NBAV targets the venom from multiple species of snakes that produce neurotoxic effects, including the Bungarus multicinctus.

This polypeptide chain is cross-linked by five disulfide bridges, categorizing the α-bungarotoxin as a type II α-neurotoxin within the three-finger toxin family.

Arginine and lysine can participate in interactions with negatively charged molecules or residues, so they may play a role in the binding to specific receptors or substrates.

[15] Similar to other α-neurotoxins within the three-finger toxin family, α-bungarotoxin exhibits a tertiary structure that is characterized by three projecting "finger" loops, a C-terminal tail, and a small globular core stabilized by four disulfide bonds.

Notably, an additional disulfide bond is present in the second loop, facilitating a proper binding through the mobility of the tips of fingers I and II.

The α-bungarotoxin polypeptide chain shows significant sequence homology with other neurotoxins from cobra and sea snake venoms, particularly with the α-toxin from Naja nivea.

Comparing α-bungarotoxin with these homologous toxins from cobra and sea snake venoms, it was revealed that there is a high degree of conservation in certain residues.

For example, α-cobra toxin, erabutoxin A,[17] and candoxin[18] contain three adjacent loops coming up from a globular, small and hydrophobic core that is cross-linked by four conserved disulfide bridges.

[15][16] Lastly, the abundance of the disulfide bonds and the limited secondary structure that is observed in the α-bungarotoxin explains its exceptional stability, which makes it resistant to denaturation even under extreme conditions such as boiling and exposure to strong acids.

By fluorescently labelling the chemically synthesised peptide it was shown it has the same effect and functionality on the nicotinic receptors as the naturally occurring α-bungarotoxin.

The venom of snakes contains numerous proteins and peptide toxins that exhibit high affinity and specificity for a larger range of receptors.

[25] In the central and peripheral nervous system, α-bungarotoxin acts by inducing paralysis in skeletal muscles by binding to a subtype of nicotinic receptors α7.

[26] From the same toxin family of Bungarotoxins (BTX), κ-BTX was shown to act postsynaptically on α3 and α4 neuronal nicotinic receptors with little effect on the muscular nAChRs, targeted by α-BTX.

Additionally, knowing it binds to nAChRs, it can be predicted where the neurotoxin would be present: neuromuscular junctions, autonomic ganglia, peripheral nerves, and adrenal medulla.

[26] In addition, by knowing the different and specific binding sites, researchers are able to visualize and track receptor localization and dynamics within cells.

This technique has been shown to be easy with the use of a 13-amino acid (WRYYESSLEPYPD) [35] mimotope, which forms a high affinity α-bungarotoxin binding site with the receptors.

Through techniques like fluorophore or enzyme conjugation followed by microscopy or immunohistochemical staining, respectively, could give insights about the complex organization and function of the nervous system.

Finally, exogenously administered α-bungarotoxin showed to penetrate the spinal cord tissue and bind to its specific sites after 7 days.

One study found that 5 mirograms/ml of the toxin completely blocks the endplate potential and extrajunctional acetylcholine sensitivity of surface fibers, within approximately 35 minutes in normal and chronically denervated muscles.

They performed a washout period of 6.5 hours, which resulted in a partial recovery of the endplate potential, with an amplitude of 0.72 +/- 0.033 mV in normal muscles.

α-Bungarotoxin binds best to the acetylholine alpha-subunit containing aromatic amino acid residues at positions 187 and 189 - e.g. shrews, cats and mice.

[40] In humans, exposure to α-bungarotoxin can lead to various symptoms, such as headache, dizziness, unconsciousness, visual and speech disturbances, and occasionally seizures.

Then, folklore medicine utilized plant-based and bioactive inhibitor compounds to treat bites from venomous animals like snakes and scorpions.

Today, treatment for krait bites involves antivenom, which can lead to various undesirable and potentially life-threatening side effects, such as nausea, urticarial, hypotension, cyanosis, and severe allergic reactions.

[42] α-Bungarotoxin belongs to a group of bungarotoxins, which are a type of poisonous proteins found in the venom of kraits - among the six most deadly snakes in Asia.