Related Experiment Video
Updated: May 3, 2026

08:09
A Technique to Functionalize and Self-assemble Macroscopic Nanoparticle-ligand Monolayer Films onto Template-free Substrates
Published on: May 9, 2014
10.4K
Facile co-assembly process to generate core-shell nanoparticles with functional protein corona
Nisaraporn Suthiwangcharoen1, Tao Li, Laying Wu
1Department of Chemistry and Biochemistry, University of South Carolina , Columbia, South Carolina 29208, United States.
Biomacromolecules
|February 13, 2014
Summary
A new method uses polymer-protein core-shell nanoparticles (PPCS-NPs) to protect protein structure. This approach enhances the activity of enzymes like glucose oxidase (GOX) and horseradish peroxidase (HRP) when combined.
Area of Science:
- Materials Science
- Biotechnology
- Nanotechnology
Background:
- Maintaining protein structure and function in nanomaterials is challenging.
- Polymer-protein interactions are key to developing stable nanostructures.
Purpose of the Study:
- To develop a protocol for creating stable polymer-protein core-shell nanoparticles (PPCS-NPs).
- To utilize PPCS-NPs as a scaffold for enzyme immobilization and activity enhancement.
Main Methods:
- Self-assembly of proteins onto water-insoluble polymers with pyridine groups.
- Structural analysis using Field Emission Scanning Electron Microscopy (FESEM) and Transmission Electron Microscopy (TEM).
- Immobilization of glucose oxidase (GOX) and horseradish peroxidase (HRP) onto PPCS-NPs.
Main Results:
- Proteins were successfully localized on the corona of PPCS-NPs, preserving their structure and conformation.
- The polymer microenvironment balanced hydrophobicity/hydrophilicity and hydrogen bonding to stabilize proteins.
- The immobilized GOX-HRP bienzymatic system exhibited a ~20% increase in activity compared to free enzymes.
Conclusions:
- A robust method for creating stable PPCS-NPs that maintain protein integrity was established.
- PPCS-NPs offer a versatile platform for biomolecule immobilization and enhancing enzymatic activity.
- This approach can be extended to various biomolecules for diverse applications.
More Related Videos
Related Concept Videos
Protein Complex Assembly
12.5K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
12.5K
Protein Complex Assembly
1.6K
1.6K
Colloidal precipitates
5.7K
The high insolubility of some precipitates can result in an unfavorable relative supersaturation. This can lead to colloidal particles with a large surface-to-mass ratio, where adsorption is promoted. For instance, in the precipitation of silver chloride, silver ions are adsorbed on the surface of the colloidal particles, forming a primary layer. This layer attracts ions of opposite charge (such as nitrate ions), forming a diffuse secondary layer of adsorbed ions. This electric double layer...
5.7K

