Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

11.5K
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,...
11.5K
Amyloid Fibrils03:03

Amyloid Fibrils

6.2K
6.2K
Alzheimer's Disease: Treatment01:22

Alzheimer's Disease: Treatment

722
Alzheimer's Disease (AD), a neurodegenerative disorder, is pathologically identified by amyloid plaques and neurofibrillary tangles composed of tau protein. AD pharmacotherapy aims to manage cognitive symptoms, delay disease progression, and treat behavioral symptoms. The treatment is primarily symptomatic and palliative, with no definitive disease-modifying therapy available. Cholinesterase inhibitors, including donepezil (Aricept), rivastigmine (Exelon), and galantamine (Razadyne), are...
722

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Aβ<sub>40</sub> Improves Cerebrovascular Endothelial Function via NOX4-Dependent Hydrogen Peroxide Release.

International journal of molecular sciences·2025
Same author

Genomic and Spectroscopic Signature-Based Discovery of Natural Macrolactams.

Journal of the American Chemical Society·2023
Same author

Antitumor Activity of Piceamycin by Upregulation of N-Myc Downstream-Regulated Gene 1 in Human Colorectal Cancer Cells.

Journal of natural products·2022
Same author

Periplocin exerts antitumor activity by regulating Nrf2-mediated signaling pathway in gemcitabine-resistant pancreatic cancer cells.

Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie·2022
Same author

Undescribed isoquinolines from Zanthoxylum nitidum and their antiproliferative effects against human cancer cell lines.

Phytochemistry·2022
Same author

Targeted Discovery of an Enediyne-Derived Cycloaromatized Compound, Jejucarboside A, from a Marine Actinomycete.

Organic letters·2022

Related Experiment Video

Updated: Jan 4, 2026

A11-positive &#946;-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
06:17

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

Published on: May 22, 2018

12.4K

Polyphenolic Biflavonoids Inhibit Amyloid-Beta Fibrillation and Disaggregate Preformed Amyloid-Beta Fibrils.

Erika Y Choi1, Sam Sik Kang2, Sang Kook Lee2

  • 1Department of Pharmacology, A.T. Still University of Health Sciences, Kirksville, MO 63501, USA.

Biomolecules & Therapeutics
|November 8, 2019
PubMed
Summary

Amentoflavone, a natural biflavonoid, effectively inhibits Alzheimer's disease amyloid-beta (Aβ) fibril formation and disassembles existing fibrils. This compound shows potent anti-amyloidogenic effects, offering potential therapeutic strategies for Alzheimer's disease.

Keywords:
Alzheimer's diseaseAmyloid β (Aβ)BiflavonoidsDisaggregationFibrillizationStructure-activity relationship

More Related Videos

Analysis of &#946;-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
06:27

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Published on: November 30, 2018

9.7K
Preparation of Oligomeric &#946;-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices
04:41

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices

Published on: July 14, 2010

23.8K

Related Experiment Videos

Last Updated: Jan 4, 2026

A11-positive &#946;-amyloid Oligomer Preparation and Assessment Using Dot Blotting Analysis
06:17

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

Published on: May 22, 2018

12.4K
Analysis of &#946;-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
06:27

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Published on: November 30, 2018

9.7K
Preparation of Oligomeric &#946;-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices
04:41

Preparation of Oligomeric β-amyloid1-42 and Induction of Synaptic Plasticity Impairment on Hippocampal Slices

Published on: July 14, 2010

23.8K

Area of Science:

  • Neuroscience
  • Biochemistry
  • Pharmacology

Background:

  • Alzheimer's disease (AD) is a leading cause of dementia, characterized by amyloid-beta (Aβ) fibril deposition in the brain.
  • Natural polyphenolic flavonoids show promise in inhibiting Aβ fibril formation and destabilizing existing aggregates.

Purpose of the Study:

  • To investigate the structure-activity relationship of naturally occurring biflavonoids in inhibiting Aβ amyloidogenesis.
  • To identify potent biflavonoids that can prevent Aβ fibril formation and disrupt preformed fibrils.

Main Methods:

  • Utilized an in vitro thioflavin T assay with Aβ1-42 peptide to assess fibrillization inhibition and disassembly.
  • Conducted atomic force microscopy (AFM) to visualize the structural effects of biflavonoids on Aβ fibrils.
  • Performed structure-activity relationship analysis of tested biflavonoid compounds.

Main Results:

  • Amentoflavone demonstrated the most potent inhibition of Aβ1-42 fibrillization (IC50: 0.26 µM) and disassembly of preformed fibrils (EC50: 0.59 µM).
  • Hydroxyl groups on biflavonoid compounds were found to be crucial for their interaction with Aβ1-42 fibrillization.
  • AFM imaging confirmed that amentoflavone disrupts the structure of mature Aβ1-42 fibrils, converting them into amorphous aggregates.

Conclusions:

  • Amentoflavone exhibits significant anti-amyloidogenic properties, targeting both the formation and structure of Aβ fibrils.
  • The findings highlight amentoflavone as a promising natural compound for therapeutic intervention in Alzheimer's disease.
  • Structure-activity relationship insights provide a basis for designing novel anti-amyloid agents.