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|Title:||Synthesis and characterization of amino acid deletion analogs of κ-hefutoxin 1, a scorpion toxin on potassium channels|
Amino acid deletion
Voltage-gated potassium channel
|Citation:||Peigneur, S., Yamaguchi, Y., Goto, H., Srinivasan, K.N., Gopalakrishnakone, P., Tytgat, J., Sato, K. (2013-09-01). Synthesis and characterization of amino acid deletion analogs of κ-hefutoxin 1, a scorpion toxin on potassium channels. Toxicon 71 : 25-30. ScholarBank@NUS Repository. https://doi.org/10.1016/j.toxicon.2013.05.010|
|Abstract:||Nine analogs of scorpion toxin peptide κ-hefutoxin 1 were synthesized by stepwise deletion of its amino acid residues. Disulfide bond pairings of the synthetic analogs were confirmed by enzymatic digestion followed by MALDI-TOF-MS measurements. Functional characterization shows that analogs in which N-terminal residues were deleted retained biological activity, whereas deletion of middle part residues resulted in loss of activity. Furthermore, κ-hefutoxin 1 and analogs were subjected to a screening on voltage-gated potassium channels in order to determine their subtype selectivity. It is shown that κ-hefutoxin 1 is suitable as template for peptidomimetics in order to design small peptide-based therapeutic compounds. © 2013 Elsevier Ltd.|
|Appears in Collections:||Staff Publications|
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