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Amyloid Fibrils

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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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Internal Energy

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The internal energy of a thermodynamic system is the sum of the kinetic and potential energies of all the molecules or entities in the system. The kinetic energy of an individual molecule includes contributions due to its rotation and vibration, as well as its translational energy. The potential energy is associated only with the interactions between one molecule and the other molecules of the system. Neither the system's location nor its motion is of any consequence as far as the internal...

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Related Experiment Video

Updated: Jan 30, 2026

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

Published on: March 27, 2017

Biflavonoids can Potentially Inhibit Amyloid Beta Internalization to Mitigate Its Cytotoxic Events.

Md Aminul Haque¹, Md Selim Hossain^2,3, Vijay Sankar Ramasamy²

¹School of Pharmacy, BRAC University, Merul Badda, Dhaka, Bangladesh.

Molecular Nutrition & Food Research

|January 29, 2026

Summary

Biflavonoids inhibit Alzheimer's disease pathology by blocking amyloid-beta 42 (Aβ42) internalization and aggregation. These natural compounds offer potential cytoprotective effects against Aβ42-induced cell death.

Keywords:

Aβ42 internalization amyloid‐β‐42 biflavonoids caspase activation cytoprotection lamin B fragmentation

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Last Updated: Jan 30, 2026

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

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Published on: March 27, 2017

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Methods to Assess Beta Cell Death Mediated by Cytotoxic T Lymphocytes

Methods to Assess Beta Cell Death Mediated by Cytotoxic T Lymphocytes

Published on: June 16, 2011

Area of Science:

Neuroscience
Biochemistry
Pharmacology

Background:

Alzheimer's disease (AD) is characterized by the accumulation of amyloid-beta 42 (Aβ42).
Aβ42 internalization into cells contributes significantly to AD pathology and neurotoxicity.
Natural compounds are being explored for their therapeutic potential in AD.

Purpose of the Study:

To investigate the potential of biflavonoids to inhibit Aβ42 uptake.
To determine if biflavonoids can mitigate Aβ42-induced cytotoxicity.
To explore the mechanisms by which biflavonoids affect Aβ42.

Main Methods:

Biochemical assays and imaging analyses were used to assess Aβ42 internalization.
Confocal microscopy and Western blotting were employed to confirm Aβ42 entry.
Cell-free aggregation assays were conducted to evaluate Aβ42 fibril, oligomer, and β-sheet formation.

Main Results:

Biflavonoids demonstrated a dose-dependent inhibition of Aβ42 internalization.
The compounds prevented lamin fragmentation and caspase activation, key markers of Aβ42-induced cell death.
Biflavonoids suppressed the formation of Aβ42 fibrils, oligomers, and β-sheets in vitro.

Conclusions:

Biflavonoids exert cytoprotective effects by inhibiting both Aβ42 conformational changes and cellular uptake.
These findings highlight biflavonoids as promising anti-amyloidogenic agents for Alzheimer's disease therapy.