Evidence map›Paper›PMID 40652042›Full record

ArticleScientific reports2025

The dynamics of oxygenation to Aβ fibrils using an azobenzene-boron complex type photocatalyst and light energy.

Yuichi Kawai, Mai Kuriyama, Youhei Sohma, Motomu Kanai, Yukiko Hori, Taisuke Tomita

Abstract read
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. 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

6 authors.

Yuichi Kawai *Laboratory of Neuropathology and Neuroscience, Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan.
Mai Kuriyama *Laboratory of Neuropathology and Neuroscience, Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan.
Youhei SohmaDepartment of Medicinal Chemistry, School of Pharmaceutical Sciences, Wakayama Medical University, Wakayama, 640-8156, Japan.
Motomu KanaiLaboratory of Synthetic Organic Chemistry, Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan.
Yukiko HoriLaboratory of Neuropathology and Neuroscience, Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan. yukiko-hori@mol.f.u-tokyo.ac.jp.
Taisuke TomitaLaboratory of Neuropathology and Neuroscience, Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan. taisuke@mol.f.u-tokyo.ac.jp.

Funding

Japan Agency for Medical Research and Development 1dk0207046Japan Agency for Medical Research and Development 23dk0207061Japan Agency for Medical Research and Development 24dk0207073Japan Agency for Medical Research and Development JP19dm0307030Japan Agency for Medical Research and Development JP19jm0210058Japan Agency for Medical Research and Development JP22dm0207072Japan Agency for Medical Research and Development JP23gm6410017Japan Society for the Promotion of Science JP18K06653Japan Society for the Promotion of Science JP19H01015Japan Society for the Promotion of Science JP19K22484Japan Society for the Promotion of Science JP23H00394Japan Society for the Promotion of Science JP23H02622Japan Society for the Promotion of Science JP23H05036Japan Society for the Promotion of Science JP23H05466Japan Society for the Promotion of Science JP24K02153
6 · The paper itself

Abstract

Alzheimer disease (AD) is characterized by the deposition of amyloid fibrils, such as senile plaques, composed of amyloid β peptide (Aβ). As a novel therapeutic modality, we have previously developed an azobenzene-boron complex type photocatalyst that photo-oxygenates Aβ fibrils. And the in vivo photo-oxygenation reaction using this photocatalyst successfully reduced the Aβ fibrils in the brain. Since Aβ fibril is one of the causative molecules in the brains of AD patients, the photocatalyst is expected to be a new modality for disease-modifying therapy against AD. However, the exact relationship between light energy and photo-oxygenating activity for Aβ fibrils remains unclear. In this paper, we have demonstrated using mass spectrometric analysis that the number of oxygens added to Aβ fibrils was increased in a sigmoidal curve with the logarithm of light energy. We also showed that it depended on the total light energy, not on the irradiance. These data suggest that photo-oxygenation proceeds at even lower levels of light energy, and it may be possible to induce photo-oxygenation in areas where light penetration is difficult, such as the human brain.

Indexed as

AmyloidAmyloid beta-PeptidesAzo CompoundsBoron CompoundsLightOxygenAlzheimer DiseaseCatalysisHumansPhotochemical ProcessesAmyloidAmyloid beta-PeptidesazobenzeneAzo CompoundsBoron CompoundsOxygenAlzheimer diseaseAmyloid βClearancePhotocatalystPhoto-oxygenation

Identifiers

PMID40652042
PMCPMC12255663

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.