Fine-Tuning hIAPP Amyloidogenesis: Probing Molecular Mechanisms via Fluorinated Core Substitutions.

Artem Pavlov, Hossein Batebi, Nicklas Österlund, Kevin Pagel, Boris Schade, Mario Schubert, Roland R Netz, Beate Koksch

Abstract read

In one paragraph

Article in ACS bio & med chem Au, 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

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3 · Its place in the literature

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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

8 authors.

Artem PavlovDepartment of Chemistry and Biochemistry, Freie Universität Berlin, Berlin 14195, Germany.ORCID https://orcid.org/0009-0005-1538-6166

Hossein BatebiDepartment of Physics, Freie Universität Berlin, Berlin 14195, Germany.ORCID https://orcid.org/0000-0002-0714-9700

Nicklas ÖsterlundDepartment of Chemistry and Biochemistry, Freie Universität Berlin, Berlin 14195, Germany.ORCID https://orcid.org/0000-0003-0905-7911

Kevin PagelDepartment of Chemistry and Biochemistry, Freie Universität Berlin, Berlin 14195, Germany.ORCID https://orcid.org/0000-0001-8054-4718

Boris SchadeResearch Center of Electron Microscopy, Freie Universität Berlin, Berlin 14195, Germany.

Mario SchubertDepartment of Chemistry and Biochemistry, Freie Universität Berlin, Berlin 14195, Germany.ORCID https://orcid.org/0000-0003-0278-4091

Roland R NetzDepartment of Physics, Freie Universität Berlin, Berlin 14195, Germany.ORCID https://orcid.org/0000-0003-0147-0162

Beate KokschDepartment of Chemistry and Biochemistry, Freie Universität Berlin, Berlin 14195, Germany.ORCID https://orcid.org/0000-0002-9747-0740

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aggregation of human islet amyloid polypeptide (hIAPP, amylin) into amyloid fibrils is a hallmark of β-cell dysfunction in type 2 diabetes, yet the molecular determinants governing its aggregation pathways remain incompletely understood. Here, we investigate how systematic fluorination of Phe23a key aromatic residue within the amyloidogenic coremodulates intra- and intermolecular interactions and thereby probes hIAPP self-assembly under physiologically relevant acidic and neutral pH conditions. Using a combination of Thioflavin T kinetics, scaling-exponent analysis, pyrene fluorescence, ion mobility-mass spectrometry, circular dichroism,

Indexed as

amyloid formationaromatic interactionsfluorineIM-MSNMRnoncanonical amino acids

Identifiers

PMID42630689

DOI10.1021/acsbiomedchemau.6c00061

PMCPMC13495020

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