Sea anemone peptides

Sea anemone venoms continue to afford a range of interesting new peptides directed against a range of biological targets. The first complete genome of a sea anemone was described recently, and its complement of toxins has been subject to various analyses. Concurrently, expressed sequence tag analyses of other anemones have identified many putative peptide toxins, while transcriptomic analyses may be expected to identify even more in the near future. Venom proteomic analyses are also revealing novel peptide toxins. Of those peptides that have been isolated, synthesized, or expressed, and then characterized functionally, the majority interact with sodium or potassium channels, although peptides binding to other targets are beginning to emerge, including one that modulates TRPV1 activity. Some of these peptides, in particular those capable of selectively blocking certain potassium channels, are being developed as new therapeutic leads.