ELAPITOXIN-Ls2a (Alpha-)

Product Name:ELAPITOXIN-Ls2a (Alpha-)

Synonyms:Neurotoxin III

CAS No:75433-28-2

Purity:95%

Molar Mass:7260

Chemical Formula:C305H468N86O100S10

Storage:Store at -20 degrees Celsius

Sequence:RECYLNPHDTQTCPSGQEICYVKSWCNAWCSSRGKVLEFGCAATCPSVNTGTEIKCCSADKCNTYP

Target:nAChRs

Application:

Elapitoxin-Ls2a (Alpha-) is a potent neurotoxic peptide derived from the venom of the Australian black snake (Pseudechis porphyriacus). This toxin specifically targets the nervous system by binding to nicotinic acetylcholine receptors (nAChRs) at the neuromuscular junction, leading to the inhibition of nerve signal transmission and resulting in paralysis. Due to its high specificity and potent action, Elapitoxin-Ls2a is of significant interest in neurobiological research, particularly in studying the structure and function of ion channels and receptors. Its role in venom toxicity also provides valuable insights into the development of antivenoms and therapeutic agents targeting neuromuscular disorders.

Current Research:

Alpha-Elapitoxin-Ls2a is a 66-amino acid peptide derived from the venom of the banded sea krait (Laticauda semifasciata). It belongs to the three-finger toxin family, characterized by a unique structural motif comprising three beta-sheet loops stabilized by disulfide bridges. This structural configuration underpins its specificity and functionality in targeting nicotinic acetylcholine receptors (nAChRs).
This peptide acts as a competitive antagonist of nAChRs at the neuromuscular junction. By binding to these receptors, Alpha-Elapitoxin-Ls2a inhibits acetylcholine interaction, thereby blocking signal transmission and inducing neuromuscular paralysis. The reversible nature of its binding makes it a useful tool for dissecting the molecular mechanisms of nAChR function and neuromuscular signaling. The toxin's moderate affinity for nAChRs ensures that it effectively modulates receptor activity without the prolonged effects observed with higher-affinity neurotoxins.
Alpha-Elapitoxin-Ls2a is particularly valuable in pharmacological research aimed at understanding the dynamics of nAChRs, which play critical roles in synaptic transmission and muscle contraction. This peptide serves as a model for studying receptor-ligand interactions and has potential applications in designing therapies for conditions associated with neuromuscular dysfunction, such as myasthenia gravis and certain types of paralysis.
In addition to its role in receptor biology, Alpha-Elapitoxin-Ls2a provides insights into the evolutionary adaptations of venom peptides. The fine-tuned interaction between this toxin and nAChRs reflects the evolutionary pressures shaping venom components for prey immobilization.
The study of Alpha-Elapitoxin-Ls2a continues to advance our understanding of receptor pharmacology, offering a foundation for therapeutic development and providing a deeper appreciation of the biochemical diversity found in venomous species. This peptide remains a cornerstone for research in neurobiology and toxinology.

Reference:

Janssen, B. J., Malinauskas, T., Weir, G. A., Cader, M. Z., Siebold, C., & Jones, E. Y. (2012). Neuropilins lock secreted semaphorins onto plexins in a ternary signaling complex. Nature structural & molecular biology, 19(12), 1293-1299.