Pharmacologically active spider peptide toxins.
Advances in mass spectrometry and peptide biochemistry coupled to modern methods in electrophysiology have permitted the isolation and identification of numerous novel peptide toxins from animal venoms in recent years. These advances have also opened up the field of spider venom research, previously unexplored due to methodological limitations. Many peptide toxins from spider venoms share structural features, amino acid composition and consensus sequences that allow them to interact with related classes of cellular receptors. They have become increasingly useful agents for the study of voltage-sensitive and ligand-gated ion channels and the discrimination of their cellular subtypes. Spider peptide toxins have also been recognized as useful agents for their antimicrobial properties and the study of pore formation in cell membranes. Spider peptide toxins with nanomolar affinities for their receptors are thus promising pharmacological tools for understanding the physiological role of ion channels and as leads for the development of novel therapeutic agents and strategies for ion channel-related diseases. Their high insecticidal potency can also make them useful probes for the discovery of novel insecticide targets in the insect nervous system or for the development of genetically engineered microbial pesticides.
Corzo
G
G
Suntory Institute for Bioorganic Research, Mishima-Gun, Shimamoto-Cho, Wakayamadai 1-1-1, Osaka 618-8503, Japan. corzo@sunbor.or.jp
Escoubas
P
P
D000595:Amino Acid Sequence; D000818:Animals; D015220:Calcium Channels / Q000187:drug effects; D007473:Ion Channels / Q000187:drug effects*; D008051:Lipid Bilayers; D010455:Peptides / Q000737:chemistry / Q000494:pharmacology*; D015221:Potassium Channels / Q000187:drug effects; D017470:Receptors, Glutamate / Q000187:drug effects; D015222:Sodium Channels / Q000187:drug effects; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013111:Spider Venoms / Q000145:classification / Q000494:pharmacology*; D013112:Spiders; D014118:Toxins, Biological / Q000737:chemistry / Q000494:pharmacology*
D015220:Calcium Channels; D007473:Ion Channels; D008051:Lipid Bilayers; D010455:Peptides; D015221:Potassium Channels; D017470:Receptors, Glutamate; D015222:Sodium Channels; D013111:Spider Venoms; D014118:Toxins, Biological