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Tc1, from Tityus cambridgei , is the first member of a new subfamily of scorpion toxin that blocks K + ‐channels
Author(s) -
Batista Cesar V.F.,
Gómez-Lagunas Froylan,
Lucas Sylvia,
Possani Lourival D.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02253-5
Subject(s) - scorpion , venom , scorpion toxin , subfamily , scorpion venoms , peptide , toxin , chemistry , stereochemistry , biochemistry , gene
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.