conotoxinen

Conotoxinen are a diverse group of peptide toxins produced by the venom of marine cone snails (genus Conus). The toxins are typically 10–40 amino acids long and are heavily modified post‑translationally, resulting in the formation of multiple disulfide bridges that stabilize their three‑dimensional structures. Conotoxinen act by targeting ion channels and receptors in the nervous system, allowing the snails to immobilise prey rapidly. They are classified into several superfamilies (e.g., μ, ω, κ, δ, and ι) based on shared cysteine frameworks and sequence motifs. Each superfamily contains multiple families of conotoxin peptides, often named according to the cone snail species from which they were isolated.

The mechanism of action of conotoxinen is highly specific: μ‑conotoxins block voltage‑gated sodium channels, ω‑conotoxins inhibit presynaptic calcium channels, κ‑conotoxins block potassium channels, and ι‑conotoxinen target voltage‑gated sodium channels with a unique mode of inhibition. This selective binding explains the potent analgesic properties of certain conotoxinen, most notably ziconotide, a synthetic form of ω‑conotoxin MVIIA that is approved for the treatment of severe chronic pain.

Research on conotoxinen has expanded the understanding of ion channel pharmacology and facilitated drug development. Beyond analgesics, studies have explored their potential in treating epilepsy, migraine, and other neurological disorders. Advances in peptide synthesis and recombinant expression have enabled large‑scale production and structure‑activity relationship investigations. Conotoxinen remain a rich source of biological tools and therapeutic leads due to their exceptional potency and selectivity.