Referenced in: none

Automatically associated channels: Kv1.3

Title: Structure-function study of a chlorotoxin-chimer and its activity on Kv1.3 channels.

Authors: Isabelle Huys, Etienne Waelkens, Jan Tytgat

Journal, date & volume: J. Chromatogr. B Analyt. Technol. Biomed. Life Sci., 2004 Apr 15 , 803, 67-73

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/15025999

Abstract
Chlorotoxin has been isolated from the venom of the scorpion Leiurus quinquestriatus and characterized as a 4.1kDa peptide, containing a lysine at position 27 that is also present in many Kv-blocking toxins. Because chlorotoxin shows no affinity for Kv-channels, we intended to design, express and purify a chlorotoxin-chimer, containing the active binding site (beta-sheet) of a very potent Kv1-channel blocking peptide, agitoxin 2, by mutating three original residues in the chlorotoxin molecule. Several derivatives of the chimer, gradually missing one additional amino acid residue at the N-terminal side of the peptide, were produced and identified chromatographically. In contrast to chlorotoxin, these chimer derivatives are capable of blocking cloned Kv1-channels.