Related Experiment Video
Updated: Apr 16, 2026
08:51
Monitoring Protein Adsorption with Solid-state Nanopores
Published on: December 2, 2011
14.2K
Surface charge effects in protein adsorption on nanodiamonds
M Aramesh1, O Shimoni, K Ostrikov
1School of Physics, The University of Melbourne, Melbourne, Victoria 3010, Australia. mrtz.aramesh@gmail.com.
Nanoscale
|March 7, 2015
Summary
Protein interactions with charged nanodiamonds are driven by electrostatics. Local pH changes significantly impact protein binding and structure, influencing biomedical applications.
Area of Science:
- Materials Science
- Biophysics
- Nanotechnology
Background:
- Protein-nanoparticle interactions are crucial for biomedical applications.
- Charged nanodiamonds offer unique surface properties for biological interfaces.
Purpose of the Study:
- To investigate protein binding, adsorption kinetics, and structure on charged nanodiamonds.
- To identify the primary driving forces behind protein adsorption.
- To understand the influence of surface charge on protein conformation and behavior.
Main Methods:
- Quartz crystal microbalance with dissipation monitoring (QCM-D).
- Infrared spectroscopy.
- Utilized model proteins: bovine serum albumin and lysozyme.
Main Results:
- Electrostatic interactions dominate protein adsorption dynamics, attachment, and conformation.
- Charge-induced local pH modifications (pH 1-3 or 11-12) near nanodiamonds profoundly affect protein properties.
- Protein size influences adsorption: smaller proteins form multilayers with conformational changes, larger proteins form monolayers with minor changes.
Conclusions:
- Electrostatic forces are key to protein adsorption on charged nanodiamonds.
- Local pH modulation is a critical factor in protein-nanoparticle interactions.
- Findings advance the understanding of biofluid-nanoparticle interactions for predictive modeling.
More Related Videos
Related Concept Videos
02:35Noncovalent Attractions in Biomolecules
66.2K
Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...
66.2K
02:35Noncovalent Attractions in Biomolecules
21.0K
21.0K
01:09Colloidal precipitates
6.9K
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...
6.9K