Structural highlights
Publication Abstract from PubMedIn 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 alpha-helical hairpin fold and therefore belongs to the alpha-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 kappa-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 approximately 35 mum) to kappa-hefutoxin 1 (IC50 approximately 40 mum). We conclude that alpha-hairpinins are attractive in their simplicity as structural templates, which may be used for functional engineering and drug design. Structural similarity between defense peptide from wheat and scorpion neurotoxin permits rational functional design.,Berkut AA, Usmanova DR, Peigneur S, Oparin PB, Mineev KS, Odintsova TI, Tytgat J, Arseniev AS, Grishin EV, Vassilevski AA J Biol Chem. 2014 May 16;289(20):14331-40. doi: 10.1074/jbc.M113.530477. Epub, 2014 Mar 26. PMID:24671422[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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