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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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A11-positive β-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis

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Inhibitory Effects of 3-(4-Hydroxy-3-methoxyphenyl) Propionic Acid on Amyloid β-Peptide Aggregation In Vitro.

Makoto Mori¹, Hiroto Nakano¹, Sadao Hikishima¹

¹Department of Neurology, Kanazawa University Graduate School of Medical Sciences, Kanazawa 920-8640, Japan.

|July 29, 2025

Summary

3-(4-Hydroxy-3-methoxyphenyl) propionic acid (HMPA) inhibits amyloid-beta (Aβ) aggregation, a key factor in dementia. This study shows HMPA’s potential in preventing Aβ42 fibril formation in vitro.

Keywords:

3-(4-hydroxy-3-methoxyphenyl) propionic acid aggregation amyloid β-protein mature fibril Aβ seeds nucleation

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Published on: March 16, 2016

Area of Science:

Neuroscience
Biochemistry
Pharmacology

Background:

3-(4-Hydroxy-3-methoxyphenyl) propionic acid (HMPA) is a metabolite of polyphenols with potential brain health benefits.
HMPA's role in dementia pathogenesis, particularly its effect on amyloid-beta (Aβ) aggregation, remains unclear.
Investigating HMPA's direct impact on Aβ42 aggregation is crucial for understanding its neuroprotective potential.

Purpose of the Study:

To evaluate the inhibitory effects of HMPA on amyloid-beta 42 (Aβ42) aggregation in vitro.
To determine if HMPA can modulate the nucleation and elongation phases of Aβ42 aggregation.
To assess HMPA's potential as a therapeutic lead for neurodegenerative diseases linked to Aβ.

Main Methods:

Utilized thioflavin T (ThT) fluorescence assays to monitor Aβ42 aggregation kinetics.
Employed electron microscopy (EM) to visualize the structural changes in Aβ42 fibrils upon HMPA treatment.
Quantified the inhibitory concentration (EC50) of HMPA against low-molecular-weight (LMW) Aβ42.

Main Results:

HMPA significantly inhibited both the nucleation and elongation phases of Aβ42 aggregation.
Electron microscopy revealed shorter Aβ42 fibrils in the presence of HMPA compared to controls.
The EC50 of HMPA for inhibiting LMW Aβ42 aggregation was determined to be 5-6 mM.

Conclusions:

HMPA demonstrates inhibitory effects on Aβ42 aggregation in vitro, similar to other polyphenols.
While effective, HMPA requires relatively high concentrations for in vitro inhibition of Aβ42.
HMPA shows promise as a lead compound for developing strategies to combat Aβ-related neurodegeneration.