Structural similarity between defense peptide from wheat and scorpion neurotoxin permits rational functional designстатья

Статья опубликована в высокорейтинговом журнале

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Дата последнего поиска статьи во внешних источниках: 20 июня 2016 г.

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[1] Structural similarity between defense peptide from wheat and scorpion neurotoxin permits rational functional design / A. A. Berkut, D. R. Usmanova, S. Peigneur et al. // Journal of Biological Chemistry. — 2014. — Vol. 289, no. 20. — P. 14331–14340. 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. [ DOI ]

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