Related Experiment Video
Updated: Apr 21, 2026

10:38
Synthesis of Functionalized 10-nm Polymer-coated Gold Particles for Endothelium Targeting and Drug Delivery
Published on: January 15, 2018
14.8K
Glycosaminoglycan functionalized nanoparticles exploit glycosaminoglycan functions
James A Vassie1, John M Whitelock, Megan S Lord
1Graduate School of Biomedical Engineering, The University of New South Wales, Sydney, NSW, 2052, Australia.
Methods in Molecular Biology (Clifton, N.J.)
|October 19, 2014
Summary
We developed a method to attach heparin (a glycosaminoglycan) to cerium oxide nanoparticles (nanoceria). The functionalized nanoceria retained heparin
Area of Science:
- Materials Science
- Biotechnology
- Nanomedicine
Background:
- Nanoparticles offer diverse applications in medicine and diagnostics.
- Surface modification of nanoparticles with glycosaminoglycans (GAGs) is an emerging strategy to enhance their biological compatibility and therapeutic potential.
- Cerium oxide nanoparticles (nanoceria) are of interest due to their unique redox properties.
Purpose of the Study:
- To describe a method for functionalizing nanoceria surfaces with GAGs, specifically heparin.
- To investigate the impact of GAG functionalization on nanoparticle properties and activity.
- To evaluate the biological activity of heparin-functionalized nanoceria.
Main Methods:
- Functionalization of nanoceria using organosilane linkers (APTES, MPTMS).
- Covalent attachment of unfractionated and low molecular weight heparin to the functionalized nanoceria.
- Assessment of heparin activity using the activated partial thromboplastin time (APTT) assay.
Main Results:
- A robust method for covalently attaching heparin to nanoceria via organosilane linkers was established.
- The heparin's biological activity, as measured by APTT assay, remained unchanged after covalent attachment to nanoceria.
- This indicates that functionalized nanoceria can retain the therapeutic properties of the attached GAGs.
Conclusions:
- Heparin-functionalized nanoceria represent a promising platform for advanced biomedical applications.
- The developed method allows for the preservation of GAG activity on nanoparticle surfaces.
- Further research can explore these functionalized nanoparticles for drug delivery and imaging.
Related Concept Videos
Glycosaminoglycans
6.4K
Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
6.4K
Proteoglycans
4.0K
Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
4.0K
Matrix Proteoglycans and Glycoproteins
4.3K
Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
4.3K
Protein Glycosylation
8.2K
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Glycosylation occurs in...
8.2K
Glycocalyx and its Functions
9.1K
The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
9.1K

