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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
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Published on: September 12, 2019

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

Alice Gualerzi1, Valentina Mangolini1, Luana Forleo1,2

  • 1IRCCS Fondazione Don Carlo Gnocchi ETS, 20148 Milan, Italy.

International Journal of Molecular Sciences
|June 26, 2026
PubMed
Summary
This summary is machine-generated.

Raman spectroscopy (RS) and surface-enhanced Raman spectroscopy (SERS) offer advanced methods for detecting pathological protein aggregates like alpha-synuclein (α-syn) and amyloid-beta (Aβ) in neurodegenerative diseases.

Keywords:
Raman spectroscopyamyloid-βbiomarkersdiagnosisneurodegenerative diseasesprotein aggregationsurface-enhanced Raman spectroscopyα-synuclein

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Detection of Protein Aggregation using Fluorescence Correlation Spectroscopy
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Detection of Protein Aggregation using Fluorescence Correlation Spectroscopy

Published on: April 25, 2021

Area of Science:

  • Biochemistry and Molecular Biology
  • Neuroscience
  • Spectroscopy

Background:

  • Parkinson's disease (PD) and Alzheimer's disease (AD) are significant global health concerns.
  • Both PD and AD are characterized by insoluble protein aggregates: α-synuclein (α-syn) in PD and amyloid-β (Aβ) in AD.
  • The ordered filamentous structure of these protein aggregates is a key feature, but their direct observation in biological samples remains challenging.

Purpose of the Study:

  • To review advances in applying Raman spectroscopy (RS) and surface-enhanced Raman spectroscopy (SERS) to study pathological protein aggregates in neurological disorders.
  • To focus on the investigation of α-syn and Aβ aggregates using these spectroscopic techniques.
  • To discuss challenges and opportunities for clinical translation of Raman-based methods for neurodegenerative disease diagnosis.

Main Methods:

  • Critical review of recent technological advancements in Raman spectroscopy (RS) and surface-enhanced Raman spectroscopy (SERS).
  • Analysis of in vitro structural characterization of protein aggregates using RS and SERS.
  • Evaluation of the application of RS and SERS to biological and clinical samples, including liquid biopsies.

Main Results:

  • RS and SERS provide powerful tools for investigating the structural properties of pathological protein aggregates like α-syn and Aβ.
  • These techniques have shown promise in analyzing protein aggregates in complex biological matrices and clinical samples.
  • Recent achievements highlight the potential of RS and SERS for detecting and quantifying these aggregates in liquid biopsies.

Conclusions:

  • Raman spectroscopy and SERS are emerging as valuable techniques for the structural characterization of protein aggregates in neurodegenerative diseases.
  • Application to liquid biopsies and clinical samples shows significant potential for developing novel diagnostic approaches.
  • Standardization of protocols is crucial for the successful clinical translation of these Raman-based diagnostic methods.