Structural and functional characterisation of peptide toxins from Australian sea anemones

Sea anemones are marine organisms that produce venoms containing disulfide-rich peptides that selectively target cell surface proteins. This study investigates the structure and function of three novel peptides identified from RNA and protein sequencing of Australian sea anemones: U-AITx-Ate1, which interacts with lipid membranes and has moderate toxicity against breast cancer cells; SA8, which does not have a well-defined structure but can inhibit the human KV1.2 channel (involved in the regulation of pre- and post-synaptic membrane excitability); and Tst2, which strongly inhibited the TRPV1 channel, making it a potential candidate for pain relief and anti-inflammatory treatments.