Binding of ApoE Isoforms to Aβ Peptides and Effects on Their Fibrillization.

Merlin Sardis, Andra Noormägi, Jüri Jarvet, Astrid Gräslund, Sebastian K T S Wärmländer, Vello Tõugu, Peep Palumaa

Abstract read

In one paragraph

Article in ACS omega, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

7 authors.

Merlin SardisDepartment of Chemistry and Biotechnology, Tallinn University of Technology, Tallinn 19086, Estonia.

Andra NoormägiDepartment of Chemistry and Biotechnology, Tallinn University of Technology, Tallinn 19086, Estonia.

Jüri JarvetDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm 106 91, Sweden.ORCID https://orcid.org/0000-0002-7863-1887

Astrid GräslundDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm 106 91, Sweden.ORCID https://orcid.org/0009-0008-0486-5032

Sebastian K T S WärmländerDepartment of Biochemistry and Biophysics, Stockholm University, Stockholm 106 91, Sweden.ORCID https://orcid.org/0000-0003-3917-1838

Vello TõuguDepartment of Chemistry and Biotechnology, Tallinn University of Technology, Tallinn 19086, Estonia.

Peep PalumaaDepartment of Chemistry and Biotechnology, Tallinn University of Technology, Tallinn 19086, Estonia.ORCID https://orcid.org/0000-0002-3505-3466

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alzheimer's disease (AD) is the most widespread neurodegenerative disease, strongly linked to amyloid depositions in the brain consisting of amyloid β (Aβ) peptides. The likelihood of developing late-onset Alzheimer's disease (LOAD) is influenced by the specific isoforms of apolipoprotein E (ApoE), with ApoE4 being the strongest known genetic risk factor for LOAD. Strong evidence suggests that ApoE impacts AD by modulating Aβ aggregation and clearance, although the precise molecular mechanisms remain incompletely understood. Microscale thermophoresis (MST) is a powerful technique for characterizing molecular interactions in solution, which has been used to determine various binding constants, although not the binding of ApoE to Aβ peptides. MST results show that ApoE isoforms bind Aβ1-40 and Aβ1-42 with low micromolar affinity. For Aβ1-42, ApoE3 shows the strongest binding (

Identifiers

PMID41726734

DOI10.1021/acsomega.5c12353

PMCPMC12917682

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LicenceCC BY

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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.