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Title: Structure-function study of a chlorotoxin-chimer and its activity on Kv1.3 channels
Authors: Huys, Isabelle ×
Waelkens, Etienne
Tytgat, Jan #
Issue Date: Mar-2004
Series Title: Journal of chromatography. B, Analytical technologies in the biomedical and life sciences. vol:803 issue:1 pages:67-73
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.
URI: 
ISSN: 1570-0232
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Toxicology and Pharmacology
Laboratory of Protein Phosphorylation and Proteomics
Research Centre for Pharmaceutical Care and Pharmaco-economics (-)
Laboratory of Phosphoproteomics (-)
Research Unit KU Leuven Centre for IT & IP Law (CiTiP)
× corresponding author
# (joint) last author

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