vely to determine the pharmacology of ion channels. Four
milies of peptides have been purified from scorpion venom. In this article, the clas
ng 30–40 amino acids linked by three or four disulfide bridges, will be discussed. Evidence is provided for the existence of 12 molecular sub
milies, named α-KTx1–12, containing 49 different peptides. Because of the pharmacological divergence of these peptides, the principle of clas
s.
face=""arial"" size=""-1"" color=""black""> Cited by: | face=""arial"" size=""-1"" color=""black""> - Zeng, Xian-Chun; Peng, Fang; Luo, Feng; Zhu, Shun-Yi; Liu, Hui; Li, Wen-Xin,""Molecular cloning and characterization of four scorpion K+-toxin-like peptides: A new subfamily of venom peptides (a-KTx14) and genomic analysis of a member1""Biochimie2001pp. 883-889
fagaoam"">Bibliographic Pagefagaoam&form=pdf&file=file.pdf"">Full Text - Garcia-Valdes, Jesus; Zamudio, Fernando Z.; Toro, Ligia; Possan, Lourival D.,""Slotoxin, aKTx1.11, a new scorpion peptide blocker of MaxiK channels that differentiates between a and a+b (b1 or b4) complexes""FEBS Letters2001pp. 369-373
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