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...
Asymmetric Lipid Bilayer01:35

Asymmetric Lipid Bilayer

Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...

You might also read

Related Articles

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

Sort by
Same author

Structure of Complex Liquid-Liquid Extraction Organic Phases for Rare Earth Separations.

Langmuir : the ACS journal of surfaces and colloids·2026
Same author

The assessment and treatment of kratom dependence: findings from a physician survey in Malaysia.

The American journal of drug and alcohol abuse·2026
Same author

Recombinant protein platform for high-throughput investigation of peptide-liposome interactions via fluorescence anisotropy depolarization.

Communications chemistry·2026
Same author

Universal progression of structure and dynamics in colloidal nanocrystal gels during salt-accelerated aging.

Science advances·2026
Same author

TCRγ constant usage tunes human γδ T cell antigen sensitivity, thymic programming, and peripheral function.

Science immunology·2026
Same author

Interactive Teaching Practices Among Trained and Untrained Medical Educators: A Cross-Sectional Analysis.

Cureus·2025

Related Experiment Video

Updated: Jun 12, 2026

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
15:04

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

6.1K

α-Synuclein Sterically Stabilizes Spherical Nanoparticle-Supported Lipid Bilayers.

Peter J Chung1,2,3, Qingteng Zhang4, Hyeondo Luke Hwang2

  • 1James Franck Institute, The University of Chicago, Chicago, Illinois 60637, United States.

ACS Applied Bio Materials
|January 14, 2022
PubMed
Summary

The protein alpha-synuclein, linked to Parkinson's disease, stabilizes lipid membranes. This study shows alpha-synuclein prevents aggregation of spherical lipid bilayers, suggesting a role in membrane structure.

Keywords:
spherical nanoparticle-supported lipid bilayerssynchrotron X-ray photon correlation spectroscopy (XPCS)synchrotron small-angle X-ray scattering (SAXS)α-synuclein

More Related Videos

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time
07:56

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

Published on: May 30, 2021

3.3K
Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
08:40

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

Published on: June 23, 2022

3.1K

Related Experiment Videos

Last Updated: Jun 12, 2026

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
15:04

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

6.1K
Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time
07:56

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time

Published on: May 30, 2021

3.3K
Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
08:40

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

Published on: June 23, 2022

3.1K

Area of Science:

  • Biochemistry
  • Neuroscience
  • Materials Science

Background:

  • Alpha-synuclein (α-synuclein) is known to bind lipid membranes.
  • Its precise biological function, particularly in relation to Parkinson's disease, remains unclear.
  • Understanding α-synuclein's interaction with membranes is crucial for Parkinson's disease research.

Purpose of the Study:

  • To investigate the effect of α-synuclein on the structure and dynamics of lipid membranes.
  • To use spherical nanoparticle lipid bilayers (SSLBs) as a model for membrane organelles.
  • To explore α-synuclein's role in interorganelle interactions.

Main Methods:

  • Utilized spherical nanoparticle lipid bilayers (SSLBs) to mimic membrane organelle properties.
  • Employed small-angle X-ray scattering (SAXS) to analyze structural changes.
  • Used X-ray photon correlation spectroscopy (XPCS) to study membrane dynamics.

Main Results:

  • SSLBs formed aggregates in the absence of α-synuclein.
  • Addition of α-synuclein disrupted these aggregates.
  • This indicates α-synuclein confers steric stabilization to membrane surfaces.

Conclusions:

  • Alpha-synuclein plays a role in stabilizing lipid membrane structures.
  • This stabilization effect may be a key function of α-synuclein in cellular processes.
  • Findings provide insights into α-synuclein's involvement in Parkinson's disease pathogenesis.