Evidence map›Paper›PMID 38503834›Full record

ArticleNature chemical biology2024

Design of amyloidogenic peptide traps.

Danny D Sahtoe, Ewa A Andrzejewska, Hannah L Han, Enrico Rennella, Matthias M Schneider, Georg Meisl, Maggie Ahlrichs, Justin Decarreau, Hannah Nguyen, Alex Kang and 7 more

Open access · hybridAbstract read
In one paragraph

Article in Nature chemical biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
11.4field-weighted citation impact, top 1% of its field
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

21 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
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  10. Biomolecular Interaction Prediction: The Era of AI.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  11. De novo design of protein binders to stabilize monomeric TDP-43 and inhibit its pathological aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Using a stable protein scaffold to display peptides that bind to alpha-synuclein fibrils.Protein science : a publication of the Protein Society · 2025
    Article
  17. Review
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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

17 authors at 3 institutions in 4 countries.

Danny D SahtoeDepartment of Biochemistry, University of Washington, Seattle, WA, USA. d.sahtoe@hubrecht.eu.ORCID 0000-0001-9095-0744
Ewa A Andrzejewska *Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.ORCID 0000-0002-1421-5569
Hannah L Han *Department of Biochemistry, University of Washington, Seattle, WA, USA.ORCID 0000-0002-4787-5168
Enrico Rennella *Department of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada.
Matthias M SchneiderYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.ORCID 0000-0002-1894-1859
Georg MeislYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.ORCID 0000-0002-6562-7715
Maggie AhlrichsDepartment of Biochemistry, University of Washington, Seattle, WA, USA.ORCID 0000-0002-4793-3890
Justin DecarreauDepartment of Biochemistry, University of Washington, Seattle, WA, USA.
Hannah NguyenDepartment of Biochemistry, University of Washington, Seattle, WA, USA.ORCID 0000-0001-9696-4004
Alex KangDepartment of Biochemistry, University of Washington, Seattle, WA, USA.
Paul LevineDepartment of Biochemistry, University of Washington, Seattle, WA, USA.
Mila LambDepartment of Biochemistry, University of Washington, Seattle, WA, USA.
Xinting LiDepartment of Biochemistry, University of Washington, Seattle, WA, USA.
Asim K BeraDepartment of Biochemistry, University of Washington, Seattle, WA, USA.ORCID 0000-0001-9473-2912
Lewis E KayDepartment of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada.
Tuomas P J KnowlesYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, UK.ORCID 0000-0002-7879-0140
David BakerDepartment of Biochemistry, University of Washington, Seattle, WA, USA. dabaker@uw.edu.ORCID 0000-0001-7896-6217
University of Washington · USUniversity of Cambridge · GBUniversity of Toronto · CA

Funding

User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI MALCOLM S. CAPEL · 2018 to 2026
$34.2M
NIGMS NIH HHS P30 GM124165
6 · The paper itself

Abstract

Segments of proteins with high β-strand propensity can self-associate to form amyloid fibrils implicated in many diseases. We describe a general approach to bind such segments in β-strand and β-hairpin conformations using de novo designed scaffolds that contain deep peptide-binding clefts. The designs bind their cognate peptides in vitro with nanomolar affinities. The crystal structure of a designed protein-peptide complex is close to the design model, and NMR characterization reveals how the peptide-binding cleft is protected in the apo state. We use the approach to design binders to the amyloid-forming proteins transthyretin, tau, serum amyloid A1 and amyloid β

Indexed as

Amyloid beta-PeptidesAmino Acid SequenceAmyloidAmyloidogenic ProteinsDrug DesignHumansModels, MolecularPeptide FragmentsPeptidesPrealbuminProtein Bindingtau ProteinsAmyloidAmyloid beta-Peptidesamyloid beta-protein (1-42)Amyloidogenic ProteinsPeptide FragmentsPeptidesPrealbumintau Proteins

Identifiers

PMID38503834
PMCPMC11288891
OpenAlexW4392956053

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.