Overview of scorpion toxins specific for Na + channels and related peptides: biodiversity, structure–function relationships and evolution

• Published in: Toxicon (Oxford) Vol. 46; no. 8; pp. 831 - 844
• Main Authors: Rodríguez de la Vega, Ricardo C., Possani, Lourival D.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 15.12.2005; Elsevier Science
• Subjects: Amino Acid Sequence; Animal poisons toxicology. Antivenoms; Animals; Biological and medical sciences; Evolution, Molecular; Genetic Variation; Long-chain peptide; Medical sciences; Models, Molecular; Molecular Sequence Data; Na+ channel; Peptides - classification; Peptides - genetics; Peptides - metabolism; Peptides - pharmacology; Phylogenetic inference; Phylogeny; Scorpion toxin; Scorpion Venoms - metabolism; Scorpions - chemistry; Sequence Alignment; Sodium Channels - metabolism; Structure-Activity Relationship; Structure–function relationship; Toxicology; Na+ channel; Phylogenetic inference; Scorpion toxin; Long-chain peptide; Structure–function relationship; Scorpionides; Peptides; Phylogenetic tree; Long chain; Animal origin; Ionic channel; Review; Biodiversity; Structure-function relationship; Toxin; Arachnida; Structure activity relation; Arthropoda; Evolution; Invertebrata
• ISSN: 0041-0101; 1879-3150
• DOI: 10.1016/j.toxicon.2005.09.006

Scorpion venoms contain a large number of bioactive components. Several of the long-chain peptides were shown to be responsible for neurotoxic effects, due to their ability to recognize Na + channels and to cause impairment of channel functions. Here, we revisited the basic paradigms in the study of these peptides in the light of recent data concerning their structure–function relationships, their functional divergence and extant biodiversity. The reviewed topics include: the criteria for classification of long-chain peptides according to their function, and a revision of the state-of-the-art knowledge concerning the surface areas of contact of these peptides with known Na + channels. Additionally, we compiled a comprehensive list encompassing 191 different amino acid sequences from long-chain peptides purified from scorpion venoms. With this dataset, a phylogenetic tree was constructed and discussed taking into consideration their documented functional divergence. A critical view on problems associated with the study of these scorpion peptides is presented, drawing special attention to the points that need revision and to the subjects under intensive research at this moment, regarding scorpion toxins specific for Na + channels and the other related long-chain peptides recently described.