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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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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

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Published on: September 12, 2019

Aβ40 Aggregation under Changeable Conditions.

Jofre Seira Curto¹, Maria Rosario Fernandez¹, Josep Cladera²

¹Unitat de Bioquímica, Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, 08193 Barcelona, Spain.

International Journal of Molecular Sciences

|May 13, 2023

Summary

This summary is machine-generated.

Altered brain pH and amyloid-β-peptide (Aβ) aggregation are linked to Alzheimer's disease. This study reveals how pH influences Aβ40 aggregation, showing neutral conditions promote stable fibril formation.

Keywords:

aggregation amyloid-β-peptide charge repulsion

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Area of Science:

Biochemistry
Neuroscience
Cell Biology

Background:

Homeostasis is vital for cellular function; disruptions, particularly altered pH, are linked to neurological disorders.
Acidic conditions in the brain, specifically in endosomes and lysosomes, are associated with amyloid-β-peptide (Aβ) aggregation and Alzheimer's disease pathogenesis.
The isoelectric point of Aβ favors aggregation under acidic conditions due to reduced charge repulsion.

Purpose of the Study:

To investigate the impact of varying pH levels on the aggregation kinetics and conformational dynamics of amyloid-β-peptide 40 (Aβ40).
To explore how different aggregated conformations of Aβ40 interact and influence the overall aggregation process under diverse pH conditions.
To understand the relationship between brain pH variations, Aβ aggregation, and the development of Alzheimer's disease.

Main Methods:

Analysis of Aβ40 aggregation under a range of pH conditions, mimicking physiological and pathological brain pH.
Characterization of different macromolecular conformations formed during the aggregation process.
Assessment of the influence of neutral pH and physiological salt concentrations on aggregation rates and fibril stability.

Main Results:

Observed that different macromolecular conformations can interact, modulating the Aβ40 aggregation pathway.
Demonstrated that neutral pH and physiological salt concentrations lead to slow aggregation kinetics.
Identified the formation of ordered, stable Aβ40 fibrils with low cytotoxic effects under neutral conditions.

Conclusions:

pH is a critical factor influencing the aggregation of amyloid-β-peptide, with implications for Alzheimer's disease.
Interactions between different aggregated conformations contribute to the complexity of Aβ aggregation in various environments.
Neutral pH and physiological conditions favor the formation of less toxic, stable amyloid fibrils, offering insights into potential therapeutic strategies.