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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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Updated: Jul 12, 2025

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

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

Published on: May 22, 2018

Curcumin Reduces Amyloid Beta Oligomer Interactions with Anionic Membranes.

Chad A Sallaberry¹, Barbie J Voss¹, William B Stone¹

¹Department of Chemistry and Biochemistry, University of Colorado Colorado Springs, Colorado Springs, Colorado 80918, United States.

ACS Chemical Neuroscience

|October 31, 2023

Summary

Curcumin inhibits amyloid-beta fibrillar oligomer (FO) aggregation on anionic membranes by altering membrane structure and interacting with FO. This dual action reduces FO accumulation, offering insights into Alzheimer

Keywords:

X-ray reflectivity amyloid beta curcumin grazing incidence X-ray diffraction lipid membranes molecular dynamics

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Published on: July 14, 2010

Area of Science:

Biochemistry
Neuroscience
Materials Science

Background:

Neurodegenerative diseases like Alzheimer's involve amyloidogenic proteins, such as amyloid-beta (Aβ), forming aggregates on cell membranes.
Curcumin, a polyphenol, interacts with membranes and affects Aβ aggregation, making it a key molecule for studying these processes.

Purpose of the Study:

To investigate the interactions between curcumin, Aβ fibrillar oligomers (FO), and anionic membranes.
To elucidate the molecular mechanisms by which curcumin modulates Aβ aggregation at membrane surfaces.

Main Methods:

Utilized liquid surface X-ray scattering experiments to study membrane structure and protein-lipid interactions.
Employed molecular dynamics simulations to visualize curcumin-membrane and curcumin-Aβ interactions at the atomic level.

Main Results:

Curcumin embeds into anionic 1,2-dimyristoyl-sn-glycero-3-phosphorylglycerol (DMPG) membranes, causing disorder and thinning.
Curcumin reduced FO accumulation on DMPG membranes by approximately 66%, attributed to membrane thinning and direct interactions.
Simulations showed curcumin clustering near phenylalanine residues on membrane-bound FO.

Conclusions:

Curcumin inhibits FO interaction with anionic membranes through a combination of altering membrane properties and direct binding to the FO surface.
This study clarifies curcumin's mechanism in inhibiting amyloidogenesis via dual membrane and protein interactions.