Interactions between Serum Albumin Proteins and Polystyrene Nanoparticles
Date
2018-07-10
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Abstract
Nanoparticles (NPs) have become increasingly popular for several applications, especially regarding biomedical applications because of their unique properties. However, when a nanoparticle enters a biological medium, it is thought to become encapsulated in proteins and other biomolecules in a coating termed a “protein corona.” This coating is significant as it can change the identity and surface properties of the nanoparticle, thus affecting its fate within the biological medium. Studies on the formation of NP-protein complexes have been ongoing for years although the interactions are still not fully understood due to their dynamics and complexity. As a result, this hinders the use of NPs to their full potential in biomedical applications. The studies performed in this thesis analyze the interactions of fluorescent polystyrene nanoparticles (FS) of two different sizes with bovine serum albumin proteins (BSA) by the technique of Two-Photon Excitation Cross-correlation Spectroscopy (TPE-FCCS). These interactions were explored both thermodynamically and kinetically to gain insight into the formation of the early hard corona and the kinetics of the formation of the BSA-FS complexes. The results suggested very low binding ratios and a mechanism of protein association dependent on the size of the sphere present in solution. The results also suggested an irreversible formation of BSA-FS complexes, in which the BSA appears to stack at the surface of the FS. These findings are significant as they challenge the current beliefs on the formation of a protein corona and perceived monolayer formation, and furthermore, provides a deeper understanding of NP-protein interactions.
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Nanoparticles, serum albumin proteins, polystyrene nanoparticles, protein corona, two-photon excitation
Citation
Bishop, A. I. (2018). Interactions between Serum Albumin Proteins and Polystyrene Nanoparticles (Master's thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca. doi:10.11575/PRISM/32363