Evidence map›Paper›PMID 39854227›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2025

Lipid-induced condensate formation from the Alzheimer's Aβ peptide triggers amyloid aggregation.

Greta Šneiderienė, Alicia González Díaz, Sourav Das Adhikari, Jiapeng Wei, Thomas Michaels, Tomas Šneideris, Sara Linse, Michele Vendruscolo, Kanchan Garai, Tuomas P J Knowles

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Nucleation Kinetics Reveals a Distinct Biological Function Space of Biomolecular Condensates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Chameleonic Nature of Aβ: Implications for Alzheimer's and Other Amyloid Diseases.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  13. Review
  14. Review
  15. Article
  16. Review
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.

Greta Šneiderienė *Yusuf Hamied Department of Chemistry, Centre for Misfolding Diseases, University of Cambridge, Cambridge CB2 1EW, United Kingdom.ORCID 0000-0002-4585-5091
Alicia González Díaz *Yusuf Hamied Department of Chemistry, Centre for Misfolding Diseases, University of Cambridge, Cambridge CB2 1EW, United Kingdom.ORCID 0000-0002-9155-1961
Sourav Das Adhikari *Tata Institute of Fundamental Research, Hyderabad 500046, India.ORCID 0000-0001-8910-0742
Jiapeng WeiYusuf Hamied Department of Chemistry, Centre for Misfolding Diseases, University of Cambridge, Cambridge CB2 1EW, United Kingdom.ORCID 0000-0003-4146-0604
Thomas MichaelsDepartment of Biology, Institute of Biochemistry, ETH Zurich, Zurich 8093, Switzerland.
Tomas ŠneiderisYusuf Hamied Department of Chemistry, Centre for Misfolding Diseases, University of Cambridge, Cambridge CB2 1EW, United Kingdom.ORCID 0000-0001-5285-871X
Sara LinseDepartment of Biochemistry and Structural Biology, Lund University, Lund SE221 00, Sweden.ORCID 0000-0001-9629-7109
Michele VendruscoloYusuf Hamied Department of Chemistry, Centre for Misfolding Diseases, University of Cambridge, Cambridge CB2 1EW, United Kingdom.ORCID 0000-0002-3616-1610
Kanchan GaraiTata Institute of Fundamental Research, Hyderabad 500046, India.ORCID 0000-0003-3753-7699
Tuomas P J KnowlesYusuf Hamied Department of Chemistry, Centre for Misfolding Diseases, University of Cambridge, Cambridge CB2 1EW, United Kingdom.ORCID 0000-0002-7879-0140

Funding

Center for misfolding diseases N/AEC | European Research Council (ERC) FP7/2007-2013Frances and Augustus Newman Foundation N/AThe Department of Atomic Energy, Government of India CRG/2020/005527The Department of Atomic Energy, Government of India RTI 4007UKRI | Biotechnology and Biological Sciences Research Council (BBSRC) N/AUKRI | Engineering and Physical Sciences Research Council (EPSRC) EP/S023046/1
6 · The paper itself

Abstract

The onset and development of Alzheimer's disease is linked to the accumulation of pathological aggregates formed from the normally monomeric amyloid-β peptide within the central nervous system. These Aβ aggregates are increasingly successfully targeted with clinical therapies at later stages of the disease, but the fundamental molecular steps in early stage disease that trigger the initial nucleation event leading to the conversion of monomeric Aβ peptide into pathological aggregates remain unknown. Here, we show that the Aβ peptide can form biomolecular condensates on lipid bilayers both in molecular assays and in living cells. Our results reveal that these Aβ condensates can significantly accelerate the primary nucleation step in the amyloid conversion cascade that leads to the formation of amyloid aggregates. We show that Aβ condensates contain phospholipids, are intrinsically heterogeneous, and are prone to undergo a liquid-to-solid transition leading to the formation of amyloid fibrils. These findings uncover the liquid-liquid phase separation behavior of the Aβ peptide and reveal a molecular step very early in the amyloid-β aggregation process.

Indexed as

Alzheimer DiseaseAmyloidAmyloid beta-PeptidesLipid BilayersPeptide FragmentsProtein Aggregation, PathologicalHumansProtein AggregatesAmyloidAmyloid beta-PeptidesLipid BilayersPeptide FragmentsProtein Aggregatesamyloid aggregationamyloid βbiomolecular condensationliquid–liquid phase separation

Identifiers

PMID39854227
PMCPMC11789053

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.