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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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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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Mass Spectrometry: Overview01:19

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Mass spectrometry is an analytical technique used to determine the molecular mass and molecular formula of a compound. The basic principle of mass spectrometry is to generate ions from the analyte molecule and measure these ion abundances against their molecular mass. One common type of ionization, known as electron ionization or EI, bombards the analyte molecules in the gas phase with high-energy electron beams. The electron beams displace an electron from the molecule and leave behind a...
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Tandem Mass Spectrometry

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Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and reduce chemical noise during analyte detection. Instruments with multiple analyzers separated by an interaction cell enable secondary fragmentation and selected study of the fragment ions.Secondary fragmentations occur in the interaction cell and can be induced by various factors. Fragmentation induced by collision with inert gases, such as N2, Ar, He, etc., is called...
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Most elements exist in nature as a mixture of isotopes. The isotopes differ in weight due to their respective number of neutrons. The molecular weight of a molecule is different depending on the specific isotope of its elements involved. As a result, the mass spectrum of the molecule exhibits peaks from the same fragment at multiple positions. The positions of these mass signals depend on the mass differences between isotopes. Furthermore, the intensity of these signals is dependent on the...
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In mass spectroscopy, amines undergo fragmentation to give parent ions with odd molecule weights. This observed mass spectrum follows the nitrogen rule; a molecule with an odd number of nitrogen atoms produces a molecular ion with an odd molecular weight. Amines undergo fragmentation through α cleavage, producing nitrogen-containing cations—iminium ions—and alkyl radicals. Mass spectra of aromatic and cyclic aliphatic amines exhibit strong molecular ion peaks, but acyclic...
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Mass Analyzers: Overview01:13

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The mass analyzer is a crucial component of the mass spectrometer. In the ionization chamber, the vaporized sample is bombarded with a high-energy electron beam to generate a radical cation and further fragment into neutral molecules, radicals, and cations. A series of negatively charged accelerator plates accelerate the cations into the mass analyzer. The mass analyzer separates ions according to their mass-to-charge (m/z) ratios and then directs them to the detector. The common types of mass...
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A Spatial Proteomics Approach to Isolate and Analyze Amyloid Proteins Using Laser Capture Microdissection and Mass

Jennifer Aguilan1, Maxwell Horton2,3, Jeffrey E Pessin3,4

  • 1Department of Pathology, Albert Einstein College of Medicine, Bronx, NY, USA.

Methods in Molecular Biology (Clifton, N.J.)
|February 2, 2026
PubMed
Summary

Accurate amyloidosis subtyping is crucial for treatment. This study introduces a spatial proteomics protocol using laser capture microdissection and mass spectrometry for precise molecular identification in FFPE tissues.

Keywords:
Amyloid protein subtypingAmyloidosisDDADIAFAIMSLaser capture microdissectionMALDI-MSI

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Area of Science:

  • Biochemistry
  • Proteomics
  • Pathology

Background:

  • Amyloidosis involves protein fibril deposition, disrupting tissue and causing organ dysfunction.
  • Accurate amyloidogenic protein identification is vital for tailored clinical management.
  • Conventional diagnostic methods lack specificity and antibody availability, leading to misclassification.

Purpose of the Study:

  • To present a spatial proteomics protocol for precise amyloidosis subtyping.
  • To integrate laser capture microdissection (LMD) with advanced mass spectrometry (MS) techniques.
  • To analyze formalin-fixed paraffin-embedded (FFPE) tissue sections for amyloid detection.

Main Methods:

  • Integration of LMD with LC-MS/MS acquisition methods (DDA, DIA).
  • Incorporation of High-Field Asymmetric Waveform Ion Mobility Spectrometry (FAIMS) for enhanced detection.
  • Analysis of FFPE tissue sections to identify amyloid proteins and co-deposited biomarkers.

Main Results:

  • Precise excision of amyloid-rich regions from minimal tissue input.
  • Enhanced detection sensitivity and reproducibility, especially for low-abundance samples.
  • Improved proteomic coverage through the combination of FAIMS, DIA, and DDA.

Conclusions:

  • The developed protocol enables accurate molecular subtyping of amyloidosis.
  • This robust and scalable platform can inform personalized therapeutic decisions.
  • Spatial proteomics offers a powerful approach for clinical pathology diagnostics.