Evidence map›Paper›PMID 29531058›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Detection of amyloid fibrils in Parkinson's disease using plasmonic chirality.

Jatish Kumar, Hasier Eraña, Elena López-Martínez, Nathalie Claes, Víctor F Martín, Diego M Solís, Sara Bals, Aitziber L Cortajarena, Joaquín Castilla, Luis M Liz-Marzán

Open access · bronzeAbstract readVideo-Audio Media
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
15.7field-weighted citation impact, top 1% 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

58 citing papers in PubMed, 304 citations in OpenAlex.

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  6. Tunable Plasmonic Circular Dichroism of Hierarchical Chiral Assemblies.Chemistry of materials : a publication of the American Chemical Society · 2025
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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

10 authors at 6 institutions in 2 countries.

Jatish KumarCenter for Cooperative Research in Biomaterials (CIC biomaGUNE), 20014 Donostia-San Sebastian, Spain.
Hasier ErañaCenter for Cooperative Research in Biosciences (CIC bioGUNE), 48160 Derio, Bizkaia, Spain.
Elena López-MartínezCenter for Cooperative Research in Biomaterials (CIC biomaGUNE), 20014 Donostia-San Sebastian, Spain.
Nathalie ClaesElectron Microscopy for Materials Science (EMAT), University of Antwerp, B-2020 Antwerp, Belgium.
Víctor F MartínDepartamento de Tecnología de los Computadores y de las Comunicaciones, University of Extremadura, 10003 Cáceres, Spain.
Diego M SolísDepartamento de Teoría de la Señal y Comunicaciones, University of Vigo, 36301 Vigo, Spain.
Sara BalsElectron Microscopy for Materials Science (EMAT), University of Antwerp, B-2020 Antwerp, Belgium.
Aitziber L CortajarenaCenter for Cooperative Research in Biomaterials (CIC biomaGUNE), 20014 Donostia-San Sebastian, Spain.
Joaquín CastillaCenter for Cooperative Research in Biosciences (CIC bioGUNE), 48160 Derio, Bizkaia, Spain.
Luis M Liz-MarzánCenter for Cooperative Research in Biomaterials (CIC biomaGUNE), 20014 Donostia-San Sebastian, Spain; llizmarzan@cicbiomagune.es.ORCID 0000-0002-6647-1353
Ikerbasque · ESCIC biomaGUNE · ESUniversity of Antwerp · BECIC bioGUNE · ESUniversidad de Extremadura · ESUniversidade de Vigo · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloid fibrils, which are closely associated with various neurodegenerative diseases, are the final products in many protein aggregation pathways. The identification of fibrils at low concentration is, therefore, pivotal in disease diagnosis and development of therapeutic strategies. We report a methodology for the specific identification of amyloid fibrils using chiroptical effects in plasmonic nanoparticles. The formation of amyloid fibrils based on α-synuclein was probed using gold nanorods, which showed no apparent interaction with monomeric proteins but effective adsorption onto fibril structures via noncovalent interactions. The amyloid structure drives a helical nanorod arrangement, resulting in intense optical activity at the surface plasmon resonance wavelengths. This sensing technique was successfully applied to human brain homogenates of patients affected by Parkinson's disease, wherein protein fibrils related to the disease were identified through chiral signals from Au nanorods in the visible and near IR, whereas healthy brain samples did not exhibit any meaningful optical activity. The technique was additionally extended to the specific detection of infectious amyloids formed by prion proteins, thereby confirming the wide potential of the technique. The intense chiral response driven by strong dipolar coupling in helical Au nanorod arrangements allowed us to detect amyloid fibrils down to nanomolar concentrations.

Indexed as

Agedalpha-SynucleinAmyloidBrainCircular DichroismCryoelectron MicroscopyElectron Microscope TomographyFemaleGoldHumansLewy BodiesNanotubesParkinson DiseasePrionsSurface Plasmon Resonancealpha-SynucleinAmyloidGoldPrionsamyloidgold nanorodsnanoplasmonicsParkinson’s diseaseplasmonic chirality

Identifiers

PMID29531058
PMCPMC5879706
OpenAlexW2792699430

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.