Discipline: Chemistry and Chemical Sciences
Subcategory: Chemistry (not Biochemistry)
Session: 3
Room: Exhibit Hall A
MaKayla Turner - Claflin University
Co-Author(s): Omotola Shode, Lincoln University; Jennifer Iwenofu, Georgia Southern University
Gold nanoparticles are utilized in a variety of sensing and detection technologies because of their unique physical and chemical (physiochemical) properties. Their tunable size, shape, and surface charge enabling them to be use in an array of platforms. Gold nanoparticles are known to aggregate under certain conditions, particularly in the presence of salts (salt effect). Researchers have exploited the aggregation properties of AuNPs to develop sensitive colorimetric assays. In vivo, a biocorona is formed on the surface of nanoparticles. The biocorona is the result of adsorption of biological molecules, proteins, lipids, and sugars onto surface of the nanoparticles as the nanoparticles are exposed to a dynamic and complex physiological environment. The most significant corona formed is the protein corona. The adsorption of the proteins on the surface of the nanoparticle influences protein conformational dynamics and physiological function(s), nanoparticle recognition and uptake, and their intracellular location. The purpose of this study is to compare and contrast the behaviors of bare gold nanoparticles (Au) and a gold nanoparticle coated with silica (Au@SiO2) in the presence of different salts and bovine serum albumin. We used various spectroscopic techniques, uV/Vis spectroscopy, fluorescence spectroscopy, and circular dichroism to characterize the behaviors of the nanoparticles. Our results conclude that the adsorption of BSA onto gold nanoparticles prevents nanoparticle aggregation. We observed that varying the ionic strength and type of ion influences the aggregation and aggregation rate of gold nanoparticles. The conformation of proteins and the absorption of proteins on the surface of gold nanoparticles are also influenced by ionic strength. Lastly, for Au@SiO2 nanoparticles, there was no evidence of nanoparticle aggregation. Protein adsorption onto this nanoparticle changed only changed the intensity of the surface plasmon band. This information will enable us to develop design principles to synthesize an array of nanoparticles for theranostic applications. Our research laboratory has synthesized nanoparticles to disrupt AB aggregation, a protein associated with Alzheimer’s disease.
Funder Acknowledgement(s): Claflin University School of Natural Sciences and Mathematics ; SCAMP
Faculty Advisor: Derrick Swinton, deswinton@claflin.edu
Role: I participated in all parts of this research.