Related Experiment Video
Updated: May 25, 2025

08:27
A Nanobar-Supported Lipid Bilayer System for the Study of Membrane Curvature Sensing Proteins in vitro
Published on: November 30, 2022
2.8K
High-Curvature Features on Branched Nanoconstructs Circumvent Protein Corona Interference
ACS Applied Materials & Interfaces
|February 27, 2025
Summary
Nanoparticle shape, specifically nanoscale curvature, influences protein corona formation and preserves ligand functionality. Sharp, positively curved tips on DNA-gold nanostars reduce protein adsorption, enhancing DNA hybridization efficiency.
Area of Science:
- Nanotechnology
- Biomaterials Science
- Surface Chemistry
Background:
- Protein corona formation on nanoparticles is crucial for their biological interactions.
- Nanoparticle surface properties, including shape and curvature, can influence protein adsorption.
- Understanding these interactions is key for designing effective nanomaterials for biomedical applications.
Purpose of the Study:
- To investigate the impact of local nanoscale curvature on nanoparticle constructs on protein corona distribution.
- To evaluate how protein adsorption affects ligand functionality on nanoparticles with varying curvatures.
- To determine if nanoparticle curvature can be engineered to control protein interactions and maintain biological activity.
Main Methods:
- Transmission electron microscopy (TEM) to visualize protein corona distribution on DNA-gold nanostars (DNA-AuNS) and gold nanospheres (DNA-50NPs).
- Statistical analysis of protein layer thickness on regions with different curvatures (positive, neutral, negative) on DNA-AuNS.
- DNA hybridization assays using 5 nm gold nanosphere probes (5NPs) to assess ligand accessibility and functionality after protein adsorption.
Main Results:
- DNA-AuNS with positive-curvature tips (<5 nm radius) exhibited less dense and uniform protein coronas compared to DNA-50NPs.
- Protein layer thickness was significantly lower on the positive-curvature tips of DNA-AuNS than on neutral or negative curvature regions.
- DNA-AuNS with reduced protein coronas showed higher DNA hybridization efficiency, indicating preserved ligand functionality, especially at the tips.
Conclusions:
- Local nanoscale curvature is a critical determinant of protein corona distribution on nanoparticle constructs.
- Positively curved nanoparticle surfaces can mitigate protein adsorption, preserving underlying ligand accessibility.
- Engineering nanoparticle curvature offers a strategy to control protein-nanoparticle interactions and maintain functional ligand presentation for biomedical applications.
Related Concept Videos
Pinching-off of Coated Vesicles
3.1K
Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
3.1K
Mechanisms of Membrane-bending
2.6K
The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
2.6K
Generation of Straight or Branched Actin Filaments
2.8K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
2.8K
Protein-Protein Interfaces
3.6K
3.6K
Fibrous Proteins
1.9K
Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
1.9K
Protein-protein Interfaces
12.4K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
12.4K

