Evidence map›Paper›PMID 42353264›Full record

ReviewInternational journal of molecular sciences2026

Raman Spectroscopy for Probing Pathological Protein Aggregates: Potential and Perspectives for Advanced Diagnostic Applications.

Alice Gualerzi, Valentina Mangolini, Luana Forleo, Chiara Cabrini, Silvia Picciolini, Marzia Bedoni

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 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

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.

Alice GualerziIRCCS Fondazione Don Carlo Gnocchi ETS, 20148 Milan, Italy.ORCID 0000-0003-2996-5714
Valentina MangoliniIRCCS Fondazione Don Carlo Gnocchi ETS, 20148 Milan, Italy.ORCID 0000-0002-5548-7405
Luana ForleoIRCCS Fondazione Don Carlo Gnocchi ETS, 20148 Milan, Italy.ORCID 0000-0002-4669-0508
Chiara CabriniIRCCS Fondazione Don Carlo Gnocchi ETS, 20148 Milan, Italy.ORCID 0009-0002-8327-2732
Silvia PiccioliniIRCCS Fondazione Don Carlo Gnocchi ETS, 20148 Milan, Italy.ORCID 0000-0002-7592-0253
Marzia BedoniIRCCS Fondazione Don Carlo Gnocchi ETS, 20148 Milan, Italy.ORCID 0000-0003-2618-3661

Funding

Fondo di Beneficenza Intesa San Paolo B/2023/0213
6 · The paper itself

Abstract

Parkinson's disease and Alzheimer's disease are currently classified as a major global health burden, sharing a defining pathological hallmark represented by insoluble protein aggregates of α-synuclein (α-syn) and amyloid-β (Aβ), respectively. A defining characteristic of all amyloids is a highly ordered, unbranched filamentous morphology, where individual β-strands align perpendicularly to the filament axis. Despite recent technological advances, direct observation of protein conformational changes and amyloid formation in biological samples remains a challenge as well as the quantification of pathological aggregates in liquid biopsies. This review critically recapitulates the major advances in the application of Raman spectroscopy (RS) and surface-enhanced Raman spectroscopy (SERS) in the investigation of pathological protein aggregates in neurological disorders, with a focus on α-syn and Aβ. We discuss both in vitro structural characterization and the applications to biological and clinical samples, outlining the main challenges for clinical translation, including the need for standardized protocols. Recent achievements in the use of RS and SERS on liquid biopsies and other clinical samples are paving the way for further implementation of Raman-based approaches for the diagnosis of neurodegenerative disorders.

Indexed as

alpha-SynucleinAlzheimer DiseaseAmyloid beta-PeptidesNeurodegenerative DiseasesParkinson DiseaseProtein AggregatesProtein Aggregation, PathologicalSpectrum Analysis, RamanAnimalsHumansalpha-SynucleinAmyloid beta-PeptidesProtein Aggregatesamyloid-βbiomarkersdiagnosisneurodegenerative diseasesprotein aggregationRaman spectroscopysurface-enhanced Raman spectroscopyα-synuclein

Identifiers

PMID42353264
PMCPMC13300589

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.