Evidence map›Paper›PMID 30713632›Full record

ArticleChemical science2019

Photoactive chlorin e6 is a multifunctional modulator of amyloid-β aggregation and toxicity

Guy Leshem, Michal Richman, Elvira Lisniansky, Merav Antman-Passig, Maram Habashi, Astrid Gräslund, Sebastian K T S Wärmländer, Shai Rahimipour

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.3field-weighted citation impact, top 11% of its field
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

11 citing papers in PubMed, 33 citations in OpenAlex.

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  11. Membrane intercalation-enhanced photodynamic inactivation of bacteria by a metallacycle and TAT-decorated virus coat protein.Proceedings of the National Academy of Sciences of the United States of America · 2019
    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

8 authors at 2 institutions in 2 countries.

Guy LeshemDepartment of Chemistry , Bar-Ilan University , Ramat-Gan 5290002 , Israel . Email: rahimis@biu.ac.il.
Michal RichmanDepartment of Chemistry , Bar-Ilan University , Ramat-Gan 5290002 , Israel . Email: rahimis@biu.ac.il.
Elvira LisnianskyDepartment of Chemistry , Bar-Ilan University , Ramat-Gan 5290002 , Israel . Email: rahimis@biu.ac.il.
Merav Antman-PassigDepartment of Chemistry , Bar-Ilan University , Ramat-Gan 5290002 , Israel . Email: rahimis@biu.ac.il.
Maram HabashiDepartment of Chemistry , Bar-Ilan University , Ramat-Gan 5290002 , Israel . Email: rahimis@biu.ac.il.
Astrid GräslundDepartment of Biochemistry and Biophysics , Arrhenius Laboratories , Stockholm University , S-106 91 Stockholm , Sweden . Email: sebastian.warmlander@dbb.su.se.
Sebastian K T S WärmländerDepartment of Biochemistry and Biophysics , Arrhenius Laboratories , Stockholm University , S-106 91 Stockholm , Sweden . Email: sebastian.warmlander@dbb.su.se.
Shai RahimipourDepartment of Chemistry , Bar-Ilan University , Ramat-Gan 5290002 , Israel . Email: rahimis@biu.ac.il.ORCID 0000-0002-3210-1645
Bar-Ilan University · ILStockholm University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The self-assembly of Aβ to β-sheet-rich neurotoxic oligomers is a main pathological event leading to Alzheimer's disease (AD). Selective targeting of Aβ oligomers without affecting other functional proteins is therefore an attractive approach to prevent the disease and its progression. In this study, we report that photodynamic treatment of Aβ in the presence of catalytic amounts of chlorin e6 can selectively damage Aβ and inhibit its aggregation and toxicity. Chlorin e6 also reversed the amyloid aggregation process in the dark by binding its soluble and low molecular weight oligomers, as shown by thioflavin T (ThT) fluorescence and photoinduced cross-linking of unmodified protein (PICUP) methods. Using HSQC NMR spectroscopy, ThT assays, amino acid analysis, SDS/PAGE, and EPR spectroscopy, we show that catalytic amounts of photoexcited chlorin e6 selectively damage the Aβ histidine residues H6, H13, and H14, and induce Aβ cross-linking by generating singlet oxygen. In contrast, photoexcited chlorin e6 was unable to cross-link ubiquitin and α-synuclein, demonstrating its high selectivity for Aβ. By binding to the Aβ histidine residues, catalytic amounts of chlorin e6 can also inhibit the Cu

Identifiers

PMID30713632
PMCPMC6333166
OpenAlexW2895319434

What OpenQuestion holds

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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.