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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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Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

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Surface-modified magnetite nanoparticles affect lysozyme amyloid fibrillization.

A Antosova¹, M Gancar¹, Z Bednarikova¹

¹Department of Biophysics, Institute of Experimental Physics, Slovak Academy of Sciences, Košice, Slovakia.

Biochimica Et Biophysica Acta. General Subjects

|June 6, 2021

Summary

Surface-modified magnetite nanoparticles (COAT-MNPs) inhibit protein amyloid aggregation. Trisodium citrate-modified nanoparticles (TC-MNPs) were most effective at preventing and breaking down amyloid fibrils.

Keywords:

Amyloid aggregation Citric acid Gum arabic Hen egg-white lysozyme Magnetite nanoparticles Trisodium citrate

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Area of Science:

Biochemistry
Materials Science
Nanotechnology

Background:

Nanoparticle (NP) surface properties significantly influence protein amyloid aggregation.
Investigated in vitro effects of surface-modified magnetite nanoparticles (COAT-MNPs) on hen egg-white lysozyme (HEWL) amyloid fibrillization and mature fibrils.

Purpose of the Study:

To evaluate the anti-amyloid potential of trisodium citrate (TC), gum arabic (GA), and citric acid (CA) surface-modified magnetite nanoparticles (COAT-MNPs).
To understand how surface modifications impact nanoparticle interactions with amyloidogenic proteins.

Main Methods:

Physico-chemical characterization using Dynamic Light Scattering (DLS).
Amyloid inhibition and fibril destruction assessed via Thioflavin T (ThT) and tryptophan (Trp) fluorescence assays.
Morphological analysis using Atomic Force Microscopy (AFM) and Gwyddion software; cytotoxicity evaluated by Trypan Blue (TB) assay.

Main Results:

Surface modification agents alter COAT-MNP properties and anti-amyloid efficacy.
COAT-MNPs inhibit fibrillization by interacting with early protein aggregates (nuclei and oligomers).
COAT-MNPs can disrupt mature amyloid fibrils by interacting with hydrophobic residues, destabilizing beta-sheet structures.

Conclusions:

COAT-MNPs effectively inhibit HEWL fibrillization and degrade mature fibrils.
Trisodium citrate-modified nanoparticles (TC-MNPs) demonstrated the highest potency among the tested COAT-MNPs.
Nanoparticle surface engineering is a viable strategy to modulate protein amyloid aggregation.