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Amyloid Fibrils

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.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...

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Single-Molecule Orientation Imaging Reveals Two Distinct Binding Configurations on Amyloid Fibrils.

Aranyak Sarkar^1,2, Vinu Namboodiri¹, Manoj Kumbhakar^1,2

¹Radiation & Photochemistry Division, Bhabha Atomic Research Center, Mumbai 400085, India.

The Journal of Physical Chemistry Letters

|May 23, 2023

Summary

This study reveals new amyloid fibril binding configurations using nanoscale imaging. An out-of-plane binding mode, driven by amino groups, offers novel strategies for developing anchored fluorescent probes.

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Area of Science:

Biophysics
Materials Science
Nanotechnology

Background:

Fluorescence signals from amyloid fibril sensors are influenced by molecular interactions and the fibril's local environment.
Understanding probe binding configurations is crucial for accurate amyloid fibril characterization.

Purpose of the Study:

To investigate the organization of amyloid fibril nanostructures and probe binding configurations.
To explore novel binding modes beyond conventional surface interactions.

Main Methods:

Utilized polarized points accumulation for imaging in nanoscale topography (PAINT).
Employed intramolecular charge transfer (ICT) probes transiently bound to amyloid fibrils.
Analyzed probe dipole orientations to determine binding configurations.

Main Results:

Identified both in-plane (parallel to fibril axis) and out-of-plane (θ < 60°) dipole populations.
Observed that over 60% of probes exhibited an out-of-plane configuration with varying mobility.
Correlated confined out-of-plane dipoles with binding within inner fibril channels and flexible dipoles with surface binding.

Conclusions:

The study highlights a significant out-of-plane binding mode for probes on amyloid fibrils.
The electron donor amino group plays a critical role in enabling this out-of-plane binding and fluorescence detection.
This finding suggests the potential for developing novel anchored probes in addition to traditional groove binders for amyloid sensing.