Evidence map›Paper›PMID 34811552›Full record

ArticleNature nanotechnology2022

De novo design of a nanopore for single-molecule detection that incorporates a β-hairpin peptide.

Keisuke Shimizu, Batsaikhan Mijiddorj, Masataka Usami, Ikuro Mizoguchi, Shuhei Yoshida, Shiori Akayama, Yoshio Hamada, Akifumi Ohyama, Kenji Usui, Izuru Kawamura and 1 more

Abstract read
In one paragraph

Article in Nature nanotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing 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

51 citing papers in PubMed.

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  12. Parametrically guided design of beta barrels and transmembrane nanopores using deep learning.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Review
  14. Article
  15. Native globular ferritin nanopore sensor.Nature communications · 2025
    Article
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  20. Article
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

11 authors.

Keisuke ShimizuDepartment of Biotechnology and Life Science, Tokyo University of Agriculture and Technology (TUAT), Tokyo, Japan.
Batsaikhan MijiddorjGraduate School of Engineering, Yokohama National University, Yokohama, Japan.
Masataka UsamiDepartment of Biotechnology and Life Science, Tokyo University of Agriculture and Technology (TUAT), Tokyo, Japan.
Ikuro MizoguchiDepartment of Biotechnology and Life Science, Tokyo University of Agriculture and Technology (TUAT), Tokyo, Japan.
Shuhei YoshidaFaculty of Frontiers of Innovative Research in Science and Technology (FIRST), Konan University, Kobe, Japan.
Shiori AkayamaFaculty of Frontiers of Innovative Research in Science and Technology (FIRST), Konan University, Kobe, Japan.
Yoshio HamadaFaculty of Frontiers of Innovative Research in Science and Technology (FIRST), Konan University, Kobe, Japan.ORCID http://orcid.org/0000-0002-2602-6917
Akifumi OhyamaGraduate School of Engineering Science, Yokohama National University, Yokohama, Japan.
Kenji UsuiFaculty of Frontiers of Innovative Research in Science and Technology (FIRST), Konan University, Kobe, Japan.ORCID http://orcid.org/0000-0003-4558-5762
Izuru KawamuraGraduate School of Engineering, Yokohama National University, Yokohama, Japan.ORCID http://orcid.org/0000-0002-8163-9695
Ryuji KawanoDepartment of Biotechnology and Life Science, Tokyo University of Agriculture and Technology (TUAT), Tokyo, Japan. rjkawano@cc.tuat.ac.jp.ORCID http://orcid.org/0000-0001-6523-0649

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The amino-acid sequence of a protein encodes information on its three-dimensional structure and specific functionality. De novo design has emerged as a method to manipulate the primary structure for the development of artificial proteins and peptides with desired functionality. This paper describes the de novo design of a pore-forming peptide, named SV28, that has a β-hairpin structure and assembles to form a stable nanopore in a bilayer lipid membrane. This large synthetic nanopore is an entirely artificial device for practical applications. The peptide forms multidispersely sized nanopore structures ranging from 1.7 to 6.3 nm in diameter and can detect DNAs. To form a monodispersely sized nanopore, we redesigned the SV28 by introducing a glycine-kink mutation. The resulting redesigned peptide forms a monodisperse pore with a diameter of 1.7 nm leading to detection of a single polypeptide chain. Such de novo design of a β-hairpin peptide has the potential to create artificial nanopores, which can be size adjusted to a target molecule.

Indexed as

NanoporesSingle Molecule ImagingAmino Acid SequenceDNAHydrophobic and Hydrophilic InteractionsIon Channel GatingLipid BilayersLysineModels, MolecularPeptidesProtein Structure, SecondaryDNALipid BilayersLysinePeptides

Identifiers

PMID34811552
PMCPMC8770118

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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.