Tc1, from Tityus cambridgei, is the first member of a new subfamily of scorpion toxin that blocks K+‐channels
César V.F. Batista, Froylán Gómez‐Lagunas, Sylvia M. Lucas, Lourival D. Possani
Abstract
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César V.F. Batista, Froylán Gómez‐Lagunas, Sylvia M. Lucas, Lourival D. Possani
Abstract
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A new peptide, Tc1, containing only 23 amino acids closely packed by three disulfide bridges was isolated from the Amazonian scorpion Tityus cambridgei. It blocks reversibly the Shaker B K(+)-channels with a K(d) of 65 nM and displaces binding of noxiustoxin to mouse brain synaptosome membranes. It is the shortest known peptide from scorpion venom that recognizes K(+)-channels and constitutes a new structural subfamily of toxin, classified as alphaKTx 13.1.
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A new peptide, Tc1, containing only 23 amino acids closely packed by three disulfide bridges was isolated from the Amazonian scorpion Tityus cambridgei. It blocks reversibly the Shaker B K(+)-channels with a K(d) of 65 nM and displaces binding of noxiustoxin to mouse brain synaptosome membranes. It is the shortest known peptide from scorpion venom that recognizes K(+)-channels and constitutes a new structural subfamily of toxin, classified as alphaKTx 13.1.
Key concepts: Scorpion, Venom, Scorpion toxin, Subfamily, Scorpion Venoms, Peptide, Toxin, Chemistry