Proteomics of the neurotoxic fraction from the sea anemone Bunodosoma cangicum venom: Novel peptides belonging to new classes of toxins

Sea Anemone Peptide with Uncommon β-Hairpin Structure Inhibits Acid-sensing Ion Channel 3 (ASIC3) and Reveals Analgesic Activity

“…Their structures were partially determined through both Edman degradation and mass spectrometry (27). For one peptide, the Bcg 23.41 toxin was assumed to have an inhibitory activity on K ϩ -channels, but this was not confirmed by direct experimentation.…”

“…Thus, so far, structural class 9a of sea anemone toxins has been determined to consist of 10 related structures and common features, such as a cysteine pattern with a 1-3, 2-4 pairing and conservative residues Pro 6 , Tyr 11 , Asp 14 , Asn 18 , Val 20 , and Gly 27 . Additionally, a typical region of 15-17 corresponds to the central ␤-turn containing mainly Ser and Gly residues that are important for structure folding.…”

Combining multidimensional liquid chromatography and MALDI–TOF-MS for the fingerprint analysis of secreted peptides from the unexplored sea anemone species Phymanthus crucifer

“…The applications of genomic/transcriptomic approaches [14][15][16][17] to the study of sea anemone toxins have been accelerated since 2006, from major studies of Nematostella vectensis [18,19] and Anemonia viridis [20], and very recently from Bunodosoma granulifera [17] using for the first time the high-throughput 454 pyrosequencing technology in the study of sea anemones. Besides the genomic/transcriptomic analyses, a very limited number of peptidomic studies focused on sea anemones toxins has been performed, in Bunodosoma cangicum [21], B. granulifera and Stichodactyla helianthus [17].…”

Functional discrimination of sea anemone neurotoxins using 3D-plotting

“…In addition, structurally novel peptide toxins, such as an epidermal growth factor (EGF)-like toxin (gigantoxin I), have also been isolated from some sea anemones although their functions remain to be clarified [5]. Recent study by Zaharenko and coworkers demonstrated the possibility of using sodium channel toxins from sea anemones as tools for dissecting the biophysical properties of inactivation in voltage-gated sodium channels [18]. Cangitoxin (CGTX) is a peptide containing 48 amino acid residues and was formerly purified from Bunodosoma cangicum.…”

“…This group also reported a substitution of N16D in this peptide sample and the co-elution of an inseparable minor isoform presenting the R14H substitution. Peptides are named as CGTX-II and CGTX-III, and their effects over Nav1.1 channels in patch clamp experiments are demonstrated [18].…”