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CasNo: 936616-33-0
Overview |
Mu-conotoxins are a family of peptides found in the venom of predatory cone snails, belonging to the genus Conus. They are known for their selective inhibition of Na+ currents in skeletal muscle, making them valuable probes for investigating voltage-dependent sodium channels in excitable tissues. |
Origin and Source | Produced by cone snails, particularly as part of their venom. |
Uses | Structurally distinct from compounds like tetrodotoxin (TTX) and saxitoxin (STX), mu-conotoxins have unique arrangements of cysteine residues and lack the knottin scaffold typically observed in other conotoxins. They target muscle-specific voltage-gated sodium channels and modulate their activity, thus affecting muscle function. One specific example, mu-conotoxin Cniiic (also known as XEP-018), is a 22-amino acid peptide molecule derived from cone snail venom. It acts as a topical muscle relaxer and is considered a biomimetic peptide, mimicking the behavior of a natural peptide found in the venom of Conus consors. This peptide has potential applications in muscle relaxation therapies. |
Endplate potentials (e.p.ps) were investigated in the presence of geographutoxin II (GTXII) in the mouse phrenic nerve diaphragm preparation. This toxin preferentially blocks muscle Na+ channels which allows the study of e.p.ps in the absence of nicotinic receptor antagonists or substances to depress acetylcholine release.
The amino acid sequence of mu-conotoxin GIIIA (otherwise called geographutoxin I), a peptide having 22 amino acid residues with three disulfide bridges, was modified by replacing each residue with Ala or Lys to elucidate its active center for blocking sodium channels of skeletal muscle.
We describe a mutation in the outer vestibule region of the adult rat skeletal muscle voltage-gated Na+ channel (microliter) that dramatically alters binding of mu-conotoxin GIIIA (mu-…