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Slotoxin, αKTx1.11, a new scorpion peptide blocker of MaxiK channels that differentiates between α and α+β (β1 or β4) complexes

A novel peptide from Centruroides noxius Hoffmann scorpion venom was isolated and sequenced. The 37 amino acid peptide belongs to the charybdotoxin sub-family (αKTx1) and was numbered member 11. αKTx1.11 has 75% sequence identity with iberiotoxin and 54% with charybdotoxin. αKTx1.11 revealed specifi...

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Bibliographic Details
Published in:FEBS letters 2001-09, Vol.505 (3), p.369-373
Main Authors: Garcia-Valdes, Jesus, Zamudio, Fernando Z, Toro, Ligia, Possan, Lourival D
Format: Article
Language:English
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Summary:A novel peptide from Centruroides noxius Hoffmann scorpion venom was isolated and sequenced. The 37 amino acid peptide belongs to the charybdotoxin sub-family (αKTx1) and was numbered member 11. αKTx1.11 has 75% sequence identity with iberiotoxin and 54% with charybdotoxin. αKTx1.11 revealed specificity for mammalian MaxiK channels (hSlo), thus, was named slotoxin. Slotoxin blocks the MaxiK pore-forming α subunit reversibly (Kd=1.5 nM). Slotoxin association with α+β (β1 or β4) channels was ∼10 times slower than iberiotoxin and charybdotoxin, leading to a lack of effect on α+β4 when tested at 100 nM for 5 min. Thus, slotoxin is a better tool to distinguish MaxiK α+β complexes.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(01)02791-0