Related Experiment Video
Updated: Jan 18, 2026

Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII
Published on: August 31, 2018
Analyzing the Interaction between Two Different Types of Nanoparticles and Serum Albumin
Roxana E Cristian1, Israa J Mohammad2, Maria Mernea3
1Department of Biochemistry and Molecular Biology, Faculty of Biology, University of Bucharest, 91-95 Spl. Independentei, 050095 Bucharest, Romania. roxana.cristian95@yahoo.com.
Abstract:
Two different types of nanoparticles (silicon dioxide and titanium dioxide) were selected within this study in order to analyze the interaction with bovine and human serum albumin. These particles were characterized by transmission and scanning electron microscopy (TEM and SEM), X-ray diffraction (XRD) and energy dispersive X-ray spectroscopy (EDXS). In addition, the hydrodynamic size and the zeta potential were measured for all these nanoparticles. The serum proteins were incubated with the nanoparticles for up to one hour, and the albumin adsorption on the particle surface was investigated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The effect induced on the secondary structure of proteins was analyzed by Fourier transform infrared spectroscopy (FTIR). The results showed that albumin adsorbed on the surface of both types of nanoparticles, but in different quantities. In addition, we noticed different changes in the structure of albumin depending on the physicochemical properties of each type of particle tested. In conclusion, our study provides a comparative analysis between the different characteristics of nanoparticles and the protein corona formed on the particle surface and effects induced on protein structure in order to direct the development of "safe-by-design" nanoparticles, as their demands for research and applications continue to increase.
Related Concept Videos
Factors Affecting Protein-Drug Binding: Drug Interactions
Displacement interactions can have varying outcomes, ranging from toxicity to virtually...
Factors Affecting Protein-Drug Binding: Protein-Related Factors
The physicochemical properties of a drug play a significant role in its ability to bind to proteins. Lipophilic drugs, which dissolve in fats, oils, and lipids, can be...
Drug Distribution: Plasma Protein Binding
Drug Binding to Blood Components
HSA is the most abundant plasma protein and is vital in drug binding. It contains distinct drug-binding sites, with different drugs exhibiting affinity for specific sites. There are three main drug-binding domains for HSA: sites I, II, and III. These domains are...
Factors Affecting Protein-Drug Binding: Drug-Related Factors
One crucial factor in drug-protein binding is the drug's lipophilicity or its affinity for fat. More lipophilic drugs tend to have higher binding extents. For example, highly lipophilic drugs like cloxacillin exhibit substantial protein binding, with as much as 95% of the drug binding to proteins. In...
Factors Affecting Protein-Drug Binding: Patient-Related Factors
Age stands as a key determinant in protein-drug binding. Neonates, characterized by low albumin content, experience heightened concentrations of unbound drugs such as phenytoin and...

