Related Experiment Video
Updated: Apr 21, 2026
08:50
Stabilizing Hepatocellular Phenotype Using Optimized Synthetic Surfaces
Published on: September 26, 2014
9.6K
Assembly, postsynthetic modification and hepatocyte targeting by multiantennary, galactosylated soft structures
Anisha Thomas1, Akansha Shukla, Sri Sivakumar
1Department of Chemistry, Indian Institute of Technology Kanpur, Kanpur-208016, UP, India. sverma@iitk.ac.in.
Chemical Communications (Cambridge, England)
|November 6, 2014
Summary
Researchers developed enzyme-modifiable hollow structures using bis-galactose lysine. These supramolecular ensembles create reactive aldehyde groups for crosslinking and cell adhesion, enhancing delivery vector potential.
Area of Science:
- Biomaterials Science
- Supramolecular Chemistry
- Drug Delivery Systems
Background:
- Hollow self-assembled structures are promising for multiantennary delivery vectors.
- Enzyme-modifiable surfaces offer versatile applications in biomaterials.
- Controlled modification of delivery vectors is crucial for targeted applications.
Purpose of the Study:
- To synthesize and characterize bis-galactose lysine based supramolecular ensembles.
- To investigate the enzyme-modifiable properties of these galactose-containing structures.
- To explore the potential of these ensembles as dynamic anchors for crosslinking and cell adhesion.
Main Methods:
- Self-assembly of bis-galactose lysine to form hollow structures.
- Enzymatic modification of surface galactose moieties.
- Generation and characterization of reactive aldehyde groups.
- Assessment of crosslinking and cell adhesion capabilities.
Main Results:
- Successful synthesis of hollow, self-assembled bis-galactose lysine structures.
- Demonstration of enzyme-mediated modification of surface galactose groups.
- Generation of reactive aldehyde functionalities on the structure surface.
- Evidence of potential for crosslinking and cell adhesion applications.
Conclusions:
- Bis-galactose lysine based supramolecular ensembles are enzyme-modifiable.
- Post-synthetic modification yields reactive aldehyde groups for versatile applications.
- These structures show promise as advanced multiantennary delivery vectors.
More Related Videos
Related Concept Videos
01:24Oligosaccharide Assembly
2.6K
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Multiple sugar molecules that may or may...
2.6K
01:25Protein 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
01:05Proteoglycans
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