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Related Experiment Video

Updated: Jun 21, 2026

Imaging Amyloid Tissues Stained with Luminescent Conjugated Oligothiophenes by Hyperspectral Confocal Microscopy and Fluorescence Lifetime Imaging
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Imaging amyloid fibrils within cells using a Se-labelling strategy.

Alexandra E Porter1, Tuomas P J Knowles, Karin Muller

  • 1Department of Materials, Imperial College London, London SW7 2AZ, UK. a.porter@imperial.ac.uk

Journal of Molecular Biology
|July 29, 2009
PubMed
Summary

Researchers developed a new method to visualize amyloid fibrils within cells using selenium-doped peptides and electron microscopy. This technique aids in understanding amyloid-related diseases like Alzheimer's by revealing fibril structure and location.

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Area of Science:

  • Biophysics
  • Cell Biology
  • Neuroscience

Background:

  • Amyloid formation by peptides and proteins is linked to systemic amyloidoses and neurodegenerative diseases, including Alzheimer's disease.
  • Understanding the cellular localization and morphology of amyloid species is crucial for elucidating their pathological roles.
  • Visualizing amyloid fibrils within cells has been a significant challenge in the field.

Purpose of the Study:

  • To develop a novel approach for direct visualization of amyloid fibrils within the cellular environment.
  • To investigate the ultrastructural localization and morphology of amyloid species in situ.
  • To provide a generalizable method for imaging specific peptides and proteins in cells using electron microscopy.

Main Methods:

  • Assembly of amyloid fibrils using selenium analogues of sulfur-containing cysteine peptides.

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  • Utilizing atomic number contrast transmission electron microscopy (Z-contrast TEM) for selective detection of selenium-doped fibrils.
  • Imaging human monocyte-derived macrophage cells exposed to transthyretin amyloid fibrils.

    • Main Results:

    • Demonstrated successful visualization of amyloid fibrils directly within human monocyte-derived macrophage cells.
    • The selenium-doped fibrils were selectively detected against the carbon-rich cellular background.
    • The method leverages the facile incorporation of seleno-cysteine and seleno-methionine, analogous to X-ray diffraction techniques.

    Conclusions:

    • The developed method offers a powerful new approach to image amyloid fibrils within cells.
    • This technique facilitates the study of amyloid formation's link to disease pathology.
    • The approach is potentially generalizable for visualizing various specific peptides and proteins in cellular contexts using electron microscopy.