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Detection and Purification of Insecticidal Peptides from Scorpions and Spiders: A Rapid Method for Their Isolation from Their Crude Venoms Using MALDI-TOF-MS Analysis

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The insecticidal neurotoxins AaIT, LqhIT2, and miew-agaIV from venom of Arachnida were rapidly re-purified from their respective crude venoms using mass spectrometry analyses and two high pressure chromatographic steps. The purity of each toxin was confirmed by capillary zone electrophoresis. Each toxin was identified by mass spectrometry and their biological activity confirmed by bioassays against tobacco cutworms and mice. In addition, AaIT and LqhIT2 were partially sequenced using post-source decay mass spectrometry analysis. The spider neurotoxin miew-agaIV was identified from other isomassic peptide by fingerprint mass analysis of its tryptic fragments.
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Keywords: Agelenopsis aperta; Androctonus australis; INSECTICIDAL PEPTIDES; Leiurus quinquestriatus; LqhIT; MALDI-TOF-MS; capillary zone electrophoresis; insecticidal neurotoxins AaIT; mass spectrometry

Document Type: Review Article

Affiliations: 1-Suntory Institute for Bioorganic Research, Mishima-Gun, Shimamoto-Cho, Wakayamadai 1-1-1, Osaka 618-8503, Japan

Publication date: 2001-10-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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