ERABUTOXIN b

Product Name:ERABUTOXIN b

Synonyms:26-L-histidine erabutoxin a

CAS No:9083-23-2

Purity:95%

Molar Mass:6869

Chemical Formula:C286H451N87O94S8

Storage:Store at -20 degrees Celsius

Sequence:RICFNQHSSQPQTTKTCPSGESSCYHKQWSDFRGTIIERGCGCPTVKPGIKLSCCESEVCNN

Target:nAChRs

Application:

Erabutoxin b is a potent neurotoxin derived from the venom of the sea snake Laticauda semifasciata. This peptide toxin specifically targets nicotinic acetylcholine receptors (nAChRs) at the neuromuscular junction, where it binds competitively to the receptor's acetylcholine binding site. By blocking acetylcholine from activating the receptor, Erabutoxin b effectively inhibits synaptic transmission, leading to paralysis. It is commonly used in neurobiological research to study the function and structure of nAChRs, as well as the mechanisms of synaptic signaling. The high specificity and affinity of Erabutoxin b make it a valuable tool for exploring neurotoxic effects and the development of potential therapeutic agents targeting neuromuscular diseases.

Current Research:

Erabutoxin b, a neurotoxic peptide derived from the venom of the sea snake Laticauda semifasciata, is a well-characterized member of the three-finger toxin (3FTx) family. This 62-amino acid peptide is stabilized by multiple disulfide bridges, contributing to its remarkable structural stability and specificity for nicotinic acetylcholine receptors (nAChRs).
The primary mechanism of Erabutoxin b involves competitive inhibition of nAChRs at the neuromuscular junction. By binding to the acetylcholine-binding site, it prevents the neurotransmitter from activating the receptor, resulting in paralysis. Its high affinity and specificity for certain subtypes of nAChRs make it an essential tool in neuropharmacological research.
Erabutoxin b is extensively utilized to study the structure and function of nAChRs. Its binding kinetics have provided significant insights into receptor-ligand interactions, aiding the development of models for receptor dynamics. In addition, it is used to probe the conformational changes of nAChRs during activation and inhibition, shedding light on the mechanisms underlying synaptic transmission.
Beyond its role in receptor studies, Erabutoxin b has contributed to the understanding of venom evolution and adaptation. The toxin's specificity for prey receptors reflects the co-evolution of predator-prey interactions, making it a subject of interest in evolutionary biology.
In therapeutic research, Erabutoxin b has been investigated as a scaffold for designing novel molecules targeting nAChRs, with potential applications in neurological disorders and diseases linked to receptor dysfunction.
Erabutoxin b remains a cornerstone for advancing our knowledge of nicotinic acetylcholine receptor biology and serves as a valuable model for understanding the molecular interplay between neurotoxins and their targets. Its contributions to receptor pharmacology and structural biology continue to inform the development of targeted therapies and enhance our understanding of synaptic mechanisms.

Reference:

Low, B. W., Preston, H. S., Sato, A., Rosen, L. S., Searl, J. E., Rudko, A. D., & Richardson, J. S. (1976). Three dimensional structure of erabutoxin b neurotoxic protein: inhibitor of acetylcholine receptor. Proceedings of the National Academy of Science