Use of Venom Peptides to Probe Ion Channel Structure and Function

• Published in: The Journal of biological chemistry Vol. 285; no. 18; pp. 13315 - 13320
• Main Authors: Dutertre, Sébastien, Lewis, Richard J.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 30.04.2010; American Society for Biochemistry and Molecular Biology
• Subjects: Animals; Channels/Calcium; Channels/Ion; Channels/Potassium; Channels/Sodium; Conotoxin; Humans; Ion Channels - chemistry; Ion Channels - metabolism; Life Sciences; Minireviews; Neurobiology; Neurons and Cognition; Peptide Mapping - methods; Peptide Structure; Peptides - chemistry; Peptides - metabolism; Protein Conformation; Protein Structure and Folding; Quantitative Structure-Activity Relationship; Receptors/Membrane; Toxicology; Toxin/Channels; Venom Peptide; Venoms - chemistry; Venoms - metabolism; Channels/Sodium; Venom Peptide; Channels/Calcium; Channels/Ion; Channels/Potassium; Toxin/Channels; Conotoxin; Receptors/Membrane; Peptide Structure
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.R109.076596

Venoms of snakes, scorpions, spiders, insects, sea anemones, and cone snails are complex mixtures of mostly peptides and small proteins that have evolved for prey capture and/or defense. These deadly animals have long fascinated scientists and the public. Early studies isolated lethal components in the search for cures and understanding of their mechanisms of action. Ion channels have emerged as targets for many venom peptides, providing researchers highly selective and potent molecular probes that have proved invaluable in unraveling ion channel structure and function. This minireview highlights molecular details of their toxin-receptor interactions and opportunities for development of peptide therapeutics.