High-performance liquid chromatography matrix-assisted laser desorption/ionization time-of-flight mass spectrometry peptide fingerprinting of tarantula venoms in the genus Brachypelma: chemotaxonomic and biochemical applications.
Precise identification of arthropod species is fundamental in venom research, particularly in groups where taxonomy problems remain unsolved. High-performance liquid chromatography and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS) analysis of crude venoms of six tarantula species in the genus Brachypelma showed that the characteristic chromatographic and peptide ion profiles obtained can be used to discriminate amongst closely related species. This method permits rapid mass fingerprinting of large numbers of samples in a reproducible manner, and offers a powerful systematic tool in combination with morphological methods for the classification of tarantula species. The sensitivity and precision of the method may offer a way to solve complex taxonomic relationships not easily resolved by morphological measurements, in a non-destructive manner. Additionally, peptide mapping of crude venoms by MALDI-TOFMS will speed up the discovery of novel ligands of neuronal receptors, since major venom components of related species share a high sequence homology and are likely to possess similar pharmacological properties.
Escoubas
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Suntory Institute for Bioorganic Research, Osaka, Japan.
Célérier
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Nakajima
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D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D019075:Electrophoresis, Capillary; D005260:Female; D008297:Male; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013111:Spider Venoms / Q000737:chemistry*; D013112:Spiders / Q000145:classification / Q000378:metabolism*
D010455:Peptides; D013111:Spider Venoms