Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein Folding

Protein Folding

Protein Folding

Protein Folding

The Nucleosome Core Particle

The Nucleosome Core Particle

Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...

Protein Folding

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

Mechanisms of Membrane Domain Formation

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...

The Nucleosome Core Particle

The Nucleosome Core Particle

Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...

You might also read

Related Articles

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

Sort by

Same author

Sonofragmentation of Organic Molecular Crystals vs Strength of Materials.

The Journal of organic chemistry·2021

Same author

The Optoelectronic Nose.

Accounts of chemical research·2020

Same author

Mechanochemistry of Metal-Organic Frameworks under Pressure and Shock.

Accounts of chemical research·2020

Same author

Ultrasensitive Monitoring of Museum Airborne Pollutants Using a Silver Nanoparticle Sensor Array.

ACS sensors·2020

Same author

Magnetically Levitated Plasma Proteins.

Analytical chemistry·2020

Same author

Quantitative Imaging of Organic Ligand Density on Anisotropic Inorganic Nanocrystals.

Nano letters·2019

Search research articles

Related Experiment Video

Updated: Jun 25, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Formation and characterization of polyglutamate core-shell microspheres.

Elizabeth M Dibbern¹, Farah Jean-Jacques Toublan, Kenneth S Suslick

¹Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, USA.

Journal of the American Chemical Society

|May 18, 2006

Summary

Researchers developed new polyglutamate microspheres for targeted drug delivery. These smaller, stable vesicles offer potential for improved biocompatible and biodegradable material applications in medicine.

More Related Videos

Assembly and Characterization of Polyelectrolyte Complex Micelles

Assembly and Characterization of Polyelectrolyte Complex Micelles

Published on: March 2, 2020

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Published on: June 26, 2020

Related Experiment Videos

Last Updated: Jun 25, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Assembly and Characterization of Polyelectrolyte Complex Micelles

Assembly and Characterization of Polyelectrolyte Complex Micelles

Published on: March 2, 2020

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Published on: June 26, 2020

Area of Science:

Biomaterials Science
Nanotechnology
Drug Delivery Systems

Background:

Biocompatible and biodegradable vesicles are crucial for organ-targeted delivery of drugs and imaging agents.
Previous work demonstrated protein microspheres with hydrophobic interiors for delivering hydrophobic materials, stabilized by protein cross-linking.

Purpose of the Study:

To develop and characterize novel core-shell microspheres using polyglutamate for potential in vivo applications.
To investigate the stability and formation mechanism of these new polyglutamate microspheres.

Main Methods:

Core-shell microspheres were synthesized using polyglutamate under slightly basic pH conditions via sonication.
Particle size and stability under physiological conditions were evaluated.

Main Results:

Polyglutamate microspheres were successfully formed with a smaller size compared to previous protein-based microspheres.
These microspheres demonstrated stability under conditions relevant for in vivo use.
Microsphere stability was attributed to hydrogen bonding networks, not covalent cross-linking.

Conclusions:

Polyglutamate microspheres represent a promising new class of biocompatible and biodegradable vesicles for drug and imaging agent delivery.
The observed stability and smaller size make them suitable candidates for in vivo applications.
The formation mechanism relying on hydrogen bonding offers an alternative to covalent cross-linking for vesicle stabilization.