Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 65, Issue 1, Pages 187-200Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-007-7370-x
Keywords
cysteine-stabilized; alpha/beta-motif; cytolytic peptides; DNA cloning; gene topology; K+ channel blocker; scorpion toxin; sequence analysis
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Among the scorpion venom components whose function are poorly known or even show contrasting pharmacological results are those called orphan peptides. The most widely distributed are named beta-KTx or scorpine-like peptides. They contain three disulfide bridges with two recognizable domains: a freely moving N-terminal amino acid sequence and a tightly folded C-terminal region with a cysteine-stabilized alpha/beta (CS-alpha beta) motif. Four such peptides and three cloned genes are reported here. They were assayed for their cytolytic, antimicrobial and K+ channel-blocking activities. Two main characteristics were found: the existence of an unusual structural and functional diversity, whereby the full-length peptide can lyse cells or kill microorganisms, and a C-terminal domain containing the CS-alpha beta motif that can block K+ channels. Furthermore, sequence analyses and phylogenetic reconstructions are used to discuss the evolution of this type of peptide and to highlight the versatility of the CS-alpha beta structures.
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