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- W2080278146 abstract "In this study, we present the spatial structure of the wheat antimicrobial peptide (AMP) Tk-AMP-X2 studied using NMR spectroscopy. This peptide was found to adopt a disulfide-stabilized α-helical hairpin fold and therefore belongs to the α-hairpinin family of plant defense peptides. Based on Tk-AMP-X2 structural similarity to cone snail and scorpion potassium channel blockers, a mutant molecule, Tk-hefu, was engineered by incorporating the functionally important residues from κ-hefutoxin 1 onto the Tk-AMP-X2 scaffold. The designed peptide contained the so-called essential dyad of amino acid residues significant for channel-blocking activity. Electrophysiological studies showed that although the parent peptide Tk-AMP-X2 did not present any activity against potassium channels, Tk-hefu blocked Kv1.3 channels with similar potency (IC50 ∼ 35 μm) to κ-hefutoxin 1 (IC50 ∼ 40 μm). We conclude that α-hairpinins are attractive in their simplicity as structural templates, which may be used for functional engineering and drug design." @default.
- W2080278146 created "2016-06-24" @default.
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- W2080278146 date "2014-05-01" @default.
- W2080278146 modified "2023-10-14" @default.
- W2080278146 title "Structural Similarity between Defense Peptide from Wheat and Scorpion Neurotoxin Permits Rational Functional Design" @default.
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- W2080278146 doi "https://doi.org/10.1074/jbc.m113.530477" @default.
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