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Pharmacologically active spider peptide toxins.
Cell Mol Life Sci. 2003 Nov; 60(11):2409-26.CM

Abstract

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.

Authors+Show Affiliations

Suntory Institute for Bioorganic Research, Mishima-Gun, Shimamoto-Cho, Wakayamadai 1-1-1, Osaka 618-8503, Japan. corzo@sunbor.or.jpNo affiliation info available

Pub Type(s)

Journal Article
Review

Language

eng

PubMed ID

14625686

Citation

Corzo, G, and P Escoubas. "Pharmacologically Active Spider Peptide Toxins." Cellular and Molecular Life Sciences : CMLS, vol. 60, no. 11, 2003, pp. 2409-26.
Corzo G, Escoubas P. Pharmacologically active spider peptide toxins. Cell Mol Life Sci. 2003;60(11):2409-26.
Corzo, G., & Escoubas, P. (2003). Pharmacologically active spider peptide toxins. Cellular and Molecular Life Sciences : CMLS, 60(11), 2409-26.
Corzo G, Escoubas P. Pharmacologically Active Spider Peptide Toxins. Cell Mol Life Sci. 2003;60(11):2409-26. PubMed PMID: 14625686.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Pharmacologically active spider peptide toxins. AU - Corzo,G, AU - Escoubas,P, PY - 2003/11/20/pubmed PY - 2004/1/6/medline PY - 2003/11/20/entrez SP - 2409 EP - 26 JF - Cellular and molecular life sciences : CMLS JO - Cell Mol Life Sci VL - 60 IS - 11 N2 - 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. SN - 1420-682X UR - https://www.unboundmedicine.com/medline/citation/14625686/Pharmacologically_active_spider_peptide_toxins_ L2 - https://doi.org/10.1007/s00018-003-3108-6 DB - PRIME DP - Unbound Medicine ER -