Evidence map›Paper›PMID 24671422›Full record

ArticleThe Journal of biological chemistry2014

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

Antonina A Berkut, Dinara R Usmanova, Steve Peigneur, Peter B Oparin, Konstantin S Mineev, Tatyana I Odintsova, Jan Tytgat, Alexander S Arseniev, Eugene V Grishin, Alexander A Vassilevski

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed.

  1. Review
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  11. Pharmaceutics · 2018
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Antonina A BerkutFrom the M. M. Shemyakin and Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia, Moscow Institute of Physics and Technology (State University), Moscow 117303, Russia.
Dinara R UsmanovaFrom the M. M. Shemyakin and Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia, Moscow Institute of Physics and Technology (State University), Moscow 117303, Russia.
Steve PeigneurLaboratory of Toxicology and Pharmacology, University of Leuven, Leuven 3000, Belgium, and.
Peter B OparinFrom the M. M. Shemyakin and Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.
Konstantin S MineevFrom the M. M. Shemyakin and Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.
Tatyana I OdintsovaN. I. Vavilov Institute of General Genetics, Russian Academy of Sciences, Moscow 119991, Russia.
Jan TytgatLaboratory of Toxicology and Pharmacology, University of Leuven, Leuven 3000, Belgium, and.
Alexander S ArsenievFrom the M. M. Shemyakin and Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.
Eugene V GrishinFrom the M. M. Shemyakin and Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia.
Alexander A VassilevskiFrom the M. M. Shemyakin and Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia, avas@ibch.ru.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Protein EngineeringAnimalsAntimicrobial Cationic PeptidesDisulfidesElectrophysiological PhenomenaModels, MolecularNeurotoxinsNuclear Magnetic Resonance, BiomolecularPotassium Channel BlockersProtein Structure, SecondaryRecombinant Fusion ProteinsScorpionsTriticumAntimicrobial Cationic PeptidesDisulfidesNeurotoxinsPotassium Channel BlockersRecombinant Fusion ProteinsAntimicrobial PeptidesHairpinHefutoxinPlant DefensePotassium ChannelsProtein DesignProtein EngineeringProtein Folding

Identifiers

PMID24671422
PMCPMC4022899

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.