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

11.7K
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,...
11.7K
Amyloid Fibrils03:03

Amyloid Fibrils

6.4K
6.4K
Destabilization of Microtubules01:45

Destabilization of Microtubules

3.5K
The destabilization of microtubules can occur during different stages of the microtubule lifecycle, such as nucleation or elongation. It can take place at either end of the microtubule or in the microtubule lattices as a whole. The lifespan of individual microtubules within a cell varies according to the cell type and stage of the cell cycle. During interphase, the lifespan of the microtubule is about 30 minutes, while during cell division, it is about 15 minutes. In axonal microtubules of...
3.5K
Drugs that Destabilize Microtubules01:10

Drugs that Destabilize Microtubules

3.7K
Microtubules are dynamic structures and can be regulated by microtubule targeting agents (MTAs). Microtubule destabilizing drugs are a class of MTAs that destabilize and prevent microtubules' polymerization. Both natural and synthetic chemicals can be found under this class of drugs. Vincristine and vinblastine, two vinca alkaloids, and colchicine were among the first to be discovered. These drugs can affect cells in various ways, either by inducing a change in cell morphology, preventing...
3.7K
Peptide Bonds02:43

Peptide Bonds

82.6K
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
82.6K
Oxidation Numbers03:14

Oxidation Numbers

42.3K
In redox reactions, the transfer of electrons occurs between reacting species. Electron transfer is described by a hypothetical number called the oxidation number (or oxidation state). It represents the effective charge of an atom or element, which is assigned using a set of rules.
42.3K

You might also read

Related Articles

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

Sort by
Same author

Evaluation of Hand Hygiene Technique in Uzbekistan: First Experience from Semmelweis Scanner-Based Digital Assessment in Educational Institutions.

Healthcare (Basel, Switzerland)·2026
Same author

Machine learning to predict plasma-based CO<sub>2</sub> conversion in dielectric barrier discharge reactors.

Green chemistry : an international journal and green chemistry resource : GC·2026
Same author

Plasma-assisted CH<sub>4</sub> activation on Cu/CeO<sub>2</sub> catalysts: insights into the effect of catalyst surface and vibrational excitation.

Physical chemistry chemical physics : PCCP·2026
Same author

Effects of Nitro-Oxidative Stress on Biomolecules: Part 2-Reactive Molecular Dynamics Simulations.

Biomolecules·2025
Same author

Vibrationally excited molecule-metal surface reactions in heterogeneous and plasma catalysis: going beyond the Fridman-Macheret <i>α</i> model.

EES catalysis·2025
Same author

Plasma catalysis: what is needed to create synergy?

EES catalysis·2025
Same journal

A tri-axis optomechanical accelerometer with plasmonic MIM waveguide and structural direction-dependent optical signatures.

Scientific reports·2026
Same journal

Holographic leaky-wave antennas with independently controlled multiple counter-rotating vortex beams.

Scientific reports·2026
Same journal

Differential associations of longitudinal hearing and vision trajectories with dementia and mild cognitive impairment in older adults.

Scientific reports·2026
Same journal

Abdominal obesity and leisure-time sedentary behavior in relation to gastroesophageal reflux disease risk: a prospective cohort study from the UK Biobank.

Scientific reports·2026
Same journal

Effect of nitrogen-rich COF incorporation on the structure and separation performance of polyamide nanofiltration membranes.

Scientific reports·2026
Same journal

Withanolide A inhibits hIAPP aggregation: An In silico, biophysical, and drosophila-based In vivo validation.

Scientific reports·2026
See all related articles

Related Experiment Video

Updated: Jan 26, 2026

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation
06:34

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

Published on: March 27, 2017

12.5K

Oxidation destabilizes toxic amyloid beta peptide aggregation.

J Razzokov1, M Yusupov2, A Bogaerts2

  • 1Research Group PLASMANT, Department of Chemistry, University of Antwerp, Universiteitsplein 1, B-2610, Antwerp, Belgium. jamoliddin.razzokov@uantwerpen.be.

Scientific Reports
|April 4, 2019
PubMed
Summary
This summary is machine-generated.

Oxidation destabilizes amyloid beta (Aβ) pentamers, reducing toxic aggregation linked to Alzheimer's disease. This finding offers insights into potential therapeutic strategies for neurodegenerative disorders.

More Related Videos

Assaying &#946;-amyloid Toxicity using a Transgenic C. elegans Model
13:59

Assaying β-amyloid Toxicity using a Transgenic C. elegans Model

Published on: October 9, 2010

26.6K
Modeling Amyloid-&#946;42 Toxicity and Neurodegeneration in Adult Zebrafish Brain
10:01

Modeling Amyloid-β42 Toxicity and Neurodegeneration in Adult Zebrafish Brain

Published on: October 25, 2017

11.7K

Related Experiment Videos

Last Updated: Jan 26, 2026

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation
06:34

A Tailored HPLC Purification Protocol That Yields High-purity Amyloid Beta 42 and Amyloid Beta 40 Peptides, Capable of Oligomer Formation

Published on: March 27, 2017

12.5K
Assaying &#946;-amyloid Toxicity using a Transgenic C. elegans Model
13:59

Assaying β-amyloid Toxicity using a Transgenic C. elegans Model

Published on: October 9, 2010

26.6K
Modeling Amyloid-&#946;42 Toxicity and Neurodegeneration in Adult Zebrafish Brain
10:01

Modeling Amyloid-β42 Toxicity and Neurodegeneration in Adult Zebrafish Brain

Published on: October 25, 2017

11.7K

Area of Science:

  • Biochemistry
  • Neuroscience
  • Computational Chemistry

Background:

  • Amyloid beta (Aβ) peptide aggregation in the brain is a hallmark of Alzheimer's disease.
  • Mechanisms for destabilizing toxic Aβ aggregates are not fully understood.
  • Oxidation, particularly via cold atmospheric plasma (CAP), shows promise in degrading Aβ aggregates.

Purpose of the Study:

  • To investigate the impact of oxidation on the stability of Aβ pentamers.
  • To elucidate conformational changes in Aβ pentamers with oxidized residues.
  • To quantify the effect of oxidation on Aβ pentamer dissociation.

Main Methods:

  • Molecular dynamics simulations.
  • Umbrella sampling techniques.
  • Free energy calculations for peptide dissociation.

Main Results:

  • Oxidation induces conformational changes in Aβ pentamers.
  • Dissociation free energy of terminal peptides decreases with increased oxidation.
  • Oxidation makes Aβ pentamer aggregation less favorable.

Conclusions:

  • Oxidation is a viable mechanism for destabilizing toxic Aβ aggregates.
  • This study provides insights into inhibiting Aβ aggregation, a key factor in Alzheimer's disease.
  • Findings support oxidation-based strategies for Alzheimer's disease treatment.