Evidence map›Paper›PMID 41326459›Full record

ArticleScientific reports2025

Synthetic deformylated α-helical PSMα3 as a selective inhibitor of human amyloid aggregation.

Aleksandra Kalitnik, Alicja W Wojciechowska, Jakub W Wojciechowski, Oliwia Polańska, Przemysław Sareło, Monika Szefczyk, Małgorzata Kotulska

Abstract read
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In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

7 authors.

Aleksandra KalitnikDepartment of Biomedical Engineering, Faculty of Fundamental Problems of Technology, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, Wrocław, 50-370, Poland. aleksandra.kalitnik@pwr.edu.pl.
Alicja W WojciechowskaDepartment of Biomedical Engineering, Faculty of Fundamental Problems of Technology, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, Wrocław, 50-370, Poland.
Jakub W WojciechowskiSano Centre for Computational Medicine, Czarnowiejska 36 building C5, Kraków, 30-054, Poland.
Oliwia PolańskaDepartment of Biomedical Engineering, Faculty of Fundamental Problems of Technology, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, Wrocław, 50-370, Poland.
Przemysław SarełoDepartment of Biomedical Engineering, Faculty of Fundamental Problems of Technology, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, Wrocław, 50-370, Poland.
Monika SzefczykDepartment of Bioorganic Chemistry, Faculty of Chemistry, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, Wrocław, 50-370, Poland. monika.szefczyk@pwr.edu.pl.
Małgorzata KotulskaDepartment of Biomedical Engineering, Faculty of Fundamental Problems of Technology, Wrocław University of Science and Technology, Wybrzeże Wyspiańskiego 27, Wrocław, 50-370, Poland.

Funding

Narodowym Centrum Nauki 2019/35/B/NZ2/03997Uniwersytet Medyczny im. Piastów Slaskich we Wroclawiu SUBK.Z516.24.068
6 · The paper itself

Abstract

The α-helical peptide PSMα3 belongs to the family of phenol-soluble modulins (PSMs) produced by the Staphylococcus aureus bacteria. Synthetic deformylated PSMα3 was previously reported to not form amyloid fibrils and maintain α-helical conformation in a monomeric form for several days of incubation. In this study, we showed that deformylated PSMα3 (dfPSMα3) attenuates fibrillation of wild type human islet amyloid polypeptide (hIAPP) and protects endothelial cells from its cytotoxicity. Kinetic assays revealed a concentration-dependent delay in the lag phase, while microscopy confirmed fewer fibrils upon co-incubation of dfPSMα3 with hIAPP. ATR-FTIR analysis further indicated that dfPSMα3 prevents the β-sheet transition of hIAPP, thereby disrupting fibril formation. On the other hand, we have not observed a similar effect of dfPSMα3 on aggregation of amyloid prone region of serum amyloid A (SAA27) and hIAPP deamidated at the C-terminus (dhIAPP). Molecular modelling suggested that dfPSMα3 could interact with a broader range of amyloidogenic peptides. We showed the key role of hydrophobic interactions in mediating molecular interactions between dfPSMα3 and other short amyloid peptides. Predicted structures indicated that hydrophobic interactions between the dfPSMα3 amino acids: Phe, Leu, and Val and those of the partner protein: Ala, Phe, Ile, Leu, and Val are likely to dominate the process of dfPSMα3 binding to other peptides. In addition, we found that the anti-fibrillation efficacy of dfPSMα3 is highly selective, dependent on the target protein sequence, and extremely sensitive to its terminal alterations.

Indexed as

AmyloidIslet Amyloid PolypeptideProtein AggregatesHumansKineticsModels, MolecularProtein Conformation, alpha-HelicalStaphylococcus aureusAmyloidIslet Amyloid PolypeptideProtein AggregatesAnti-fibrillation effectCell protective effecthIAPPMolecular modellingSynthetic dfPSMα3

Identifiers

PMID41326459
PMCPMC12675706

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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.