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Related Concept Videos

Imaging Biological Samples with Optical Microscopy01:18

Imaging Biological Samples with Optical Microscopy

Optical microscopy uses optic principles to provide detailed images of samples. Antonie van Leeuwenhoek designed the first compound optical microscope in the 17th century to visualize blood cells, bacteria, and yeast cells. In 1830, Joseph Jackson Lister created an essentially modern light microscope. The 20th century saw the development of microscopes with enhanced magnification and resolution.
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Total Internal Reflection Fluorescence Microscopy

Total internal reflection fluorescence microscopy or TIRF is an advanced microscopic technique used to visualize fluorophores in samples close to a solid surface with a higher refractive index, such as a glass coverslip. TIRF only allows fluorophores in proximity to the solid surface to be excited. When light from a medium with a lower refractive index (such as air) hits the glass coverslip at a critical angle, the light undergoes total internal reflection stead of passing through the glass.
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Super-resolution Fluorescence Microscopy

Super-resolution fluorescence microscopy (SRFM) provides a better resolution than conventional fluorescence microscopy by reducing the point spread function (PSF). PSF is the light intensity distribution from a point that causes it to appear blurred. Due to PSF, each fluorescing point appears bigger than its actual size, and it is the PSF interference of nearby fluorophores that causes the blurred image. Various approaches to achieving higher resolution through SRFM have recently been developed.

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Nanoscale Chemical Imaging of Amyloid Fibrils in Water Using Total-Internal-Reflection Tip-Enhanced Raman

Yuhan Huang1, Gary S Cooney1, David Talaga1

  • 1Univ. Bordeaux, CNRS, Bordeaux INP, ISM, UMR 5255, F-33400 Talence, France.

The Journal of Physical Chemistry Letters
|October 1, 2024
PubMed
Summary

Total-internal-reflection tip-enhanced Raman spectroscopy (TIR-TERS) reveals amyloid-β fibril structure in water. Hydration has minimal impact on fibril structure, opening new biological imaging possibilities.

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Area of Science:

  • Biophysics
  • Spectroscopy
  • Materials Science

Background:

  • Amyloid-β fibrils are implicated in neurodegenerative diseases.
  • Understanding their structure in biologically relevant environments is crucial.
  • Previous studies were limited to ambient air conditions.

Purpose of the Study:

  • To perform nanoscale imaging of amyloid-β (Aβ1-42-L34T) fibrils in water using TIR-TERS.
  • To investigate the impact of hydration on amyloid fibril structure.
  • To explore the distribution of aromatic amino acids within fibrils.

Main Methods:

  • Fabrication of TERS tips via bipolar electrodeposition.
  • Total-internal-reflection tip-enhanced Raman spectroscopy (TIR-TERS) imaging in aqueous solution.
  • Theoretical simulations to optimize experimental parameters.

Main Results:

  • Nanoscale spatial resolution imaging of Aβ1-42-L34T fibrils achieved in water.
  • Predominant parallel β-sheet secondary structure identified.
  • Nanoscale distribution of tyrosine, histidine, and phenylalanine mapped.
  • Hydration shown to have a marginal effect on fibril structure.

Conclusions:

  • TIR-TERS is a viable technique for studying amyloid fibrils in liquid.
  • Amyloid fibril structure is largely preserved in aqueous environments.
  • This study provides a foundation for future biological applications of TIR-TERS.