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 Experiment Video

Updated: May 16, 2025

Chemical Dimerization-Induced Protein Condensates on Telomeres
08:52

Chemical Dimerization-Induced Protein Condensates on Telomeres

Published on: April 12, 2021

3.1K

Decoupling Phase Separation and Fibrillization Preserves Activity of Biomolecular Condensates.

Tharun Selvam Mahendran1, Anurag Singh2, Sukanya Srinivasan2

  • 1Department of Biological Sciences, The State University of New York at Buffalo, Buffalo, NY, 14260, USA.

Research Square
|May 9, 2025
PubMed
Summary

Related Concept Videos

Condensins02:15

Condensins

3.2K
Condensins are large protein complexes that use ATP to fuel the assembly of chromosomes during mitosis. They transform the tangled, shapeless mass of post-interphase DNA into individualized chromosomes by compacting, organizing, and segregating chromosomal DNA.
The plant and animal cells contain two types of condensin complexes—condensin I and condensin II. Both complexes have five subunits: two SMC (Structural Maintenance of Chromosomes) subunits, a kleisin subunit, and two HEAT-repeat...
3.2K
Protein Folding01:22

Protein Folding

116.8K
Overview
116.8K
Actin Filament Depolymerization01:19

Actin Filament Depolymerization

2.9K
Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
2.9K
¹³C NMR: ¹H–¹³C Decoupling01:04

¹³C NMR: ¹H–¹³C Decoupling

961
The probability of having two carbon-13 atoms next to each other is negligible because of the low natural abundance of carbon-13. Consequently, peak splitting due to carbon-carbon spin-spin coupling is not observed in spectra. However, protons up to three sigma bonds away split the carbon signal according to the n+1 rule, resulting in complicated spectra.
A broadband decoupling technique is used to simplify these complex, sometimes overlapping, signals. Broadband decoupling relies on a...
961
Disassembly of Intermediate Filaments01:35

Disassembly of Intermediate Filaments

2.0K
Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
Keratin proteins, found at the cell periphery near cell junctions, undergo a cycle of assembly and disassembly. In Type...
2.0K
Amyloid Fibrils03:03

Amyloid Fibrils

9.1K
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,...
9.1K

You might also read

Related Articles

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

Sort by
Same author

The Critical Role of the 2'-OH group in Phase Separation and Percolation Transitions of RNA.

bioRxiv : the preprint server for biology·2026
Same author

Decoupling phase separation and fibrillization preserves activity of biomolecular condensates.

Nature communications·2026
Same author

Viscoelasticity and interface properties of multi-component condensates govern protein sequestration and suppression of amyloid formation.

bioRxiv : the preprint server for biology·2026
Same author

Intrinsically Disordered Protein Coating for Oral Delivery of Peptide Drugs.

bioRxiv : the preprint server for biology·2025
Same author

Soft probe particle tracking microrheology using membraneless organelles to study viscoelasticity of nucleolar subcompartments.

Biointerphases·2025
Same author

Loading causes molecular damage in fibrin fibers.

Soft matter·2025

Small molecule L-arginine prevents neurodegeneration-linked Tau protein condensates from forming amyloid fibrils. This metabolite preserves condensate function by blocking the transition, offering a new therapeutic strategy.

Area of Science:

  • Biochemistry and Molecular Biology
  • Neuroscience
  • Biophysics

Background:

  • Age-dependent transformation of protein condensates into amyloid fibrils is implicated in neurodegenerative diseases.
  • The relationship between reversible protein phase separation and irreversible amyloid formation remains unclear.
  • Microtubule-associated protein Tau (Tau) forms functional, liquid-like condensates that can age into fibrils.

Purpose of the Study:

  • To investigate whether the forces driving phase separation and amyloid formation are distinct.
  • To explore if small molecules can prevent the transition of Tau condensates to amyloid fibrils.
  • To determine if preserving condensate metastability can maintain biochemical function.

Main Methods:

  • Utilized an engineered, biochemically active version of Tau protein to form liquid-like condensates.

More Related Videos

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells
06:48

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Published on: January 5, 2024

3.2K
Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

15.0K

Related Experiment Videos

Last Updated: May 16, 2025

Chemical Dimerization-Induced Protein Condensates on Telomeres
08:52

Chemical Dimerization-Induced Protein Condensates on Telomeres

Published on: April 12, 2021

3.1K
Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells
06:48

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Published on: January 5, 2024

3.2K
Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

15.0K
  • Studied the aging process of Tau condensates under quiescent, cofactor-free conditions.
  • Assessed the effect of the small molecule L-arginine on condensate-to-fibril transition and phase separation.

    • Main Results:

    • Liquid-like Tau condensates spontaneously aged into amyloid fibrils, impairing their ability to recruit tubulin and assemble microtubules.
    • L-arginine selectively inhibited the condensate-to-fibril transition without affecting phase separation.
    • L-arginine increased the fibril nucleation barrier, counteracting the age-dependent loss of Tau condensate activity.

    Conclusions:

    • Thermodynamic forces governing phase separation and amyloid maturation are separable.
    • Small molecule metabolites, like L-arginine, can enhance protein condensate metastability.
    • Metabolite intervention offers a strategy to preserve condensate function and potentially mitigate neurodegeneration.