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

12.1K
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,...
12.1K
Amyloid Fibrils03:03

Amyloid Fibrils

6.5K
6.5K

You might also read

Related Articles

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

Sort by
Same author

Clocked stepping of an artificial protein walker along a DNA track.

Nature nanotechnology·2026
Same author

Interplay of Noncovalent Interactions in Phase Separation Mediated by Tyrosine-Rich and Arginine-Rich Polypeptides.

Journal of the American Chemical Society·2026
Same author

Potent and biased agonists of class B1 GPCRs from a heterochiral design strategy.

Nature chemistry·2026
Same author

<i>De novo</i> grafted coiled-coil peptides as p53/<i>h</i>DM2 inhibitors.

RSC chemical biology·2026
Same author

Bifunctional Catalysis of a Crossed Aldol Condensation by Diamines: Impact of Tether Composition and Length.

The Journal of organic chemistry·2026
Same author

Altered Intracellular Trafficking as a Mechanism for Prolonged Duration of G Protein-Coupled Receptor Activation.

Journal of the American Chemical Society·2026

Related Experiment Video

Updated: Feb 19, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

6.5K

Toward a Soluble Model System for the Amyloid State.

Nicole C Thomas1, Gail J Bartlett2, Derek N Woolfson2,3,4

  • 1Department of Chemistry, University of Wisconsin-Madison , Madison, Wisconsin 53706, United States.

Journal of the American Chemical Society
|November 9, 2017
PubMed
Summary

Researchers developed a novel model system to study amyloid formation, crucial for understanding diseases like Alzheimer's. This system facilitates comparing sequence variants and their impact on amyloid structure and stability.

More Related Videos

Fabrication of Amyloid-&#946;-Secreting Alginate Microbeads for Use in Modelling Alzheimer's Disease
06:52

Fabrication of Amyloid-β-Secreting Alginate Microbeads for Use in Modelling Alzheimer's Disease

Published on: July 6, 2019

9.7K
Neurodegeneration in an Animal Model of Chronic Amyloid-beta Oligomer Infusion Is Counteracted by Antibody Treatment Infused with Osmotic Pumps
10:19

Neurodegeneration in an Animal Model of Chronic Amyloid-beta Oligomer Infusion Is Counteracted by Antibody Treatment Infused with Osmotic Pumps

Published on: August 14, 2016

9.7K

Related Experiment Videos

Last Updated: Feb 19, 2026

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

6.5K
Fabrication of Amyloid-&#946;-Secreting Alginate Microbeads for Use in Modelling Alzheimer's Disease
06:52

Fabrication of Amyloid-β-Secreting Alginate Microbeads for Use in Modelling Alzheimer's Disease

Published on: July 6, 2019

9.7K
Neurodegeneration in an Animal Model of Chronic Amyloid-beta Oligomer Infusion Is Counteracted by Antibody Treatment Infused with Osmotic Pumps
10:19

Neurodegeneration in an Animal Model of Chronic Amyloid-beta Oligomer Infusion Is Counteracted by Antibody Treatment Infused with Osmotic Pumps

Published on: August 14, 2016

9.7K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Disease Mechanisms

Background:

  • Amyloid formation and deposition are linked to numerous diseases.
  • Amyloids share a β-sheet secondary structure, but their inter-sheet packing differs from soluble proteins.
  • Studying amyloid aggregates is challenging due to sequence-dependent multiple conformations and packing arrangements.

Purpose of the Study:

  • To develop a minimum-sized, soluble model system for the amyloid state.
  • To enable comparative studies of different sequence variants.
  • To investigate sequence-structure relationships in amyloid formation.

Main Methods:

  • Development of a novel linking strategy for inter-sheet association.
  • Utilizing side chain interactions for mediating association, characteristic of amyloid states.
  • Designing a model system for exploring sequence variants.

Main Results:

  • Initial steps toward a functional, minimum-sized amyloid model system.
  • Identification of a linker design enabling characteristic inter-sheet association.
  • Establishment of a platform for comparing sequence variants.

Conclusions:

  • The developed model system is a crucial step towards understanding amyloid diseases.
  • The novel linker strategy facilitates the study of sequence-structure-stability relationships in amyloids.
  • This approach will aid in exploring specific strand-association modes and their impact on amyloid stability.