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

9.2K
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,...
9.2K

You might also read

Related Articles

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

Sort by
Same author

Is dUTPase Enzymatic Activity Truly Essential for Viability?

International journal of molecular sciences·2025
Same author

Authentic hSAA related with AA amyloidosis: New method of purification, folding and amyloid polymorphism.

Biophysical chemistry·2024
Same author

Co-chaperonin GroES subunit exchange as dependent on time, pH, protein concentration, and urea.

Biochimica et biophysica acta. Proteins and proteomics·2024
Same author

Bacteriophage T5 dUTPase: Combination of Common Enzymatic and Novel Functions.

International journal of molecular sciences·2024
Same author

Influence of Amino Acid Substitutions in ApoMb on Different Stages of Unfolding of Amyloids.

Molecules (Basel, Switzerland)·2023
Same author

The New Functional Hybrid Chaperone Protein ADGroEL-SacSm.

Molecules (Basel, Switzerland)·2023

Related Experiment Video

Updated: Jun 6, 2025

A11-positive β-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

11.8K

Acceleration of carbonic anhydrase amyloid aggregation leads to a decrease in the fibrils toxicity.

Liliia Fakhranurova1, Victor Marchenkov2, Anatoly Glukhov2

  • 1Branch of the Institute of Bioorganic Chemistry RAS, Prospekt Nauki, 6, Pushchino, 142290, Russia.

Biochemical and Biophysical Research Communications
|December 2, 2024
PubMed
Summary

Accelerating amyloid formation can reduce protein aggregate toxicity. Modifying residue hydrophobicity impacts amyloid structure and cytotoxicity, offering strategies against amyloid diseases.

Keywords:
Aggregation rateAmyloidCarbonic anhydraseCytotoxicityOligomers

More Related Videos

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
00:15

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

5.9K
Modified Roller Tube Method for Precisely Localized and Repetitive Intermittent Imaging During Long-term Culture of Brain Slices in an Enclosed System
09:52

Modified Roller Tube Method for Precisely Localized and Repetitive Intermittent Imaging During Long-term Culture of Brain Slices in an Enclosed System

Published on: December 28, 2017

10.6K

Related Experiment Videos

Last Updated: Jun 6, 2025

A11-positive β-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

11.8K
Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
00:15

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

5.9K
Modified Roller Tube Method for Precisely Localized and Repetitive Intermittent Imaging During Long-term Culture of Brain Slices in an Enclosed System
09:52

Modified Roller Tube Method for Precisely Localized and Repetitive Intermittent Imaging During Long-term Culture of Brain Slices in an Enclosed System

Published on: December 28, 2017

10.6K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Protein aggregates, particularly amyloid fibrils, are implicated in cellular damage and amyloid diseases.
  • Understanding the structural properties of cytotoxic amyloid fibrils is crucial for developing therapeutic strategies.

Purpose of the Study:

  • To investigate the structural characteristics of cytotoxic amyloid fibrils.
  • To identify strategies for mitigating the damaging effects of these protein aggregates.
  • To explore the relationship between protein aggregation kinetics, structure, and cytotoxicity using Bovine carbonic anhydrase B (BCAB).

Main Methods:

  • Studied the kinetics of amyloid formation for wild-type BCAB and six mutant variants.
  • Analyzed the structural features (e.g., cross-β-structure content) of mature fibrils and early globular aggregates.
  • Assessed the cytotoxicity of different aggregate forms on cells.

Main Results:

  • Increased residue hydrophobicity accelerated amyloid aggregation but resulted in fibrils with lower cross-β-structure and reduced toxicity.
  • Decreased hydrophobicity (L139A substitution) and slower aggregation initiation led to the formation of highly toxic oligomers during the lag phase.
  • Amyloid formation kinetics and protein hydrophobicity significantly influence aggregate structure and cellular toxicity.

Conclusions:

  • Accelerating amyloid formation can alter aggregate structure, leading to decreased cytotoxicity.
  • Hydrophobicity is a key factor in determining the toxic potential of amyloid aggregates.
  • Targeting aggregation pathways and structural features offers potential therapeutic avenues for amyloid diseases.