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

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, normally used to...
Amyloid Fibrils03:03

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, normally used to...

You might also read

Related Articles

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

Sort by
Same author

Data-driven modelling makes quantitative predictions regarding bacteria surface motility.

PLoS computational biology·2024
Same author

Controlled Formation of Star Polymer Nanoparticles via Visible Light Photopolymerization.

ACS macro letters·2022
Same author

A generic class of amyloid fibril inhibitors.

Journal of materials chemistry. B·2020
Same author

Shear Induced Interactions Cause Polymer Compression.

Scientific reports·2020
Same author

Polyacrylic acid based plasma fractionation for the production of albumin and IgG: Compatibility with existing commercial downstream processes.

Biotechnology and bioengineering·2020
Same author

Electrostatic Screening Length in Concentrated Salt Solutions.

Langmuir : the ACS journal of surfaces and colloids·2019
Same journal

Mapping Functional Dynamics Hotspots for Protein Engineering with NMR Peak Intensity Analysis.

Protein engineering, design & selection : PEDS·2026
Same journal

Combining bacterial display and protein language models to engineer a CD69-binding affibody for molecular imaging of immune activation.

Protein engineering, design & selection : PEDS·2026
Same journal

Examining selection dynamics and limitations in multi-round protein selection of high diversity libraries.

Protein engineering, design & selection : PEDS·2026
Same journal

A photo-enhanced oxidative coupling for site-specific protein Labeling via noncanonical amino acid incorporation.

Protein engineering, design & selection : PEDS·2026
Same journal

Engineering affibody domains as anti-idiotypic masks for nivolumab-based prodrugs.

Protein engineering, design & selection : PEDS·2026
Same journal

Integrating machine learning tools in protein design: a case of MHETase engineering for PET biodeconstruction.

Protein engineering, design & selection : PEDS·2026
See all related articles

Related Experiment Video

Updated: Jun 19, 2026

Analysis of β-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

Shear flow promotes amyloid-{beta} fibrilization.

Dave E Dunstan1, Paul Hamilton-Brown, Peter Asimakis

  • 1Department of Chemical and Biomolecular Engineering and Particulate Fluids Processing Centre, University of Melbourne, VIC 3010, Australia. davided@unimelb.edu.au

Protein Engineering, Design & Selection : PEDS
|October 24, 2009
PubMed
Summary
This summary is machine-generated.

Shear forces significantly accelerate amyloid-beta (Abeta) fibril formation in aqueous solutions. This process, observed via fluorescence and microscopy, involves structural changes from random coil to beta-sheet secondary structures.

More Related Videos

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

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

Related Experiment Videos

Last Updated: Jun 19, 2026

Analysis of β-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

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

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

Area of Science:

  • Biochemistry
  • Materials Science
  • Neuroscience

Background:

  • Amyloid fibrils are associated with neurodegenerative diseases.
  • Understanding the mechanisms of amyloid formation is crucial for developing therapeutic strategies.

Purpose of the Study:

  • To investigate the effect of shear forces on amyloid-beta (Abeta) fibril formation.
  • To elucidate the role of shearing versus simple mixing in accelerating amyloidogenesis.

Main Methods:

  • Amyloid-beta (Abeta) solutions were subjected to stirring (simulating shear) at 37°C.
  • Thioflavin T fluorescence assays were used to monitor fibril formation.
  • Atomic Force Microscopy (AFM) was employed to visualize aggregates and fibrils.
  • Circular Dichroism (CD) spectroscopy analyzed changes in protein secondary structure.

Main Results:

  • Stirring Abeta solutions at 37°C rapidly induced amyloid fibril formation, evidenced by increased thioflavin T fluorescence.
  • AFM imaging confirmed the formation, growth, and intertwining of Abeta fibrils over time.
  • CD spectroscopy revealed a structural transition from random coil to alpha-helix and then to beta-sheet secondary structures.
  • Quiescent solutions showed no amyloid formation over 3 days, indicating shear, not just incubation, is critical.
  • Couette flow experiments confirmed that shearing, not mixing, is the primary driver of accelerated amyloid formation.

Conclusions:

  • Shear forces are a potent accelerator of amyloid-beta fibril formation.
  • The observed acceleration is attributed to the mechanical effect of shearing, not simple mixing.
  • The findings suggest that mechanical forces play a significant role in protein aggregation pathways relevant to disease.