Title

Mixed-Monolayer Gold Nanoparticle Interactions with Bovine Serum Albumin

Document Type

Oral Presentation

Event Website

https://source2022.sched.com/

Start Date

18-5-2022

End Date

18-5-2022

Keywords

Engineered nanoparticles, Chemistry, biomedicine, biochemistry

Abstract

Engineered nanoparticles (ENPs) have become common in industry and commercial products and have in recent years gained further attention for their possible diagnostic and therapeutic applications in biomedicine. These applications necessitate a thorough understanding of the behavior and interactions of ENPs in vivo. It is known that nanoparticles, when they enter the bloodstream, associate with serum proteins to varying degrees, resulting in different outcomes. These associations are driven by the characteristics of the nanoparticles including size, core composition, and surface chemistry. In this study, gold nanoparticles (AuNPs) of 5 nm diameter were synthesized with monolayers composed of a negatively-charged ligand (mercaptohexanoic acid, (MHA)), a neutral ligand (mercaptoethoxyethoxy ethanol (MEEE)), or a mixture of the two ligands, and used to investigate interactions with bovine serum albumin (BSA). Fluorescence titrations were conducted to determine binding affinity and it was found that the binding constants (Ka) for MHA, MEEE, and mixed-ligand AuNPs were 0.47 ± 0.02 nM-1, 0.40 ± 0.02 nM-1, and 0.48 ± 0.02 nM-1, respectively, indicating that the affinity of BSA for both MHA-capped and mixed-ligand AuNPs is higher than that for MEEE-capped AuNPs. The difference between MHA and MEEE-capped and between mixed-ligand and MEEE-capped AuNPs was statistically significant, whereas the difference between the mixed-ligand and MHA-capped AuNPs was not. Fluorescence studies were also used to determine the Hill coefficient n for the binding of BSA with each AuNP type. In all cases n was greater than 1, indicating cooperative binding of BSA molecules to the AuNP surface.

College of the Sciences Presentation Award Winner.

Faculty Mentor(s)

Samuel Lohse

Department/Program

Chemistry

Additional Mentoring Department

Chemistry

Additional Mentoring Department

Graduate Studies

Additional Mentoring Department

Ivory Nelson Graduate Fellowship

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Mixed-Monolayer Gold Nanoparticle Interactions with Bovine Serum Albumin

Engineered nanoparticles (ENPs) have become common in industry and commercial products and have in recent years gained further attention for their possible diagnostic and therapeutic applications in biomedicine. These applications necessitate a thorough understanding of the behavior and interactions of ENPs in vivo. It is known that nanoparticles, when they enter the bloodstream, associate with serum proteins to varying degrees, resulting in different outcomes. These associations are driven by the characteristics of the nanoparticles including size, core composition, and surface chemistry. In this study, gold nanoparticles (AuNPs) of 5 nm diameter were synthesized with monolayers composed of a negatively-charged ligand (mercaptohexanoic acid, (MHA)), a neutral ligand (mercaptoethoxyethoxy ethanol (MEEE)), or a mixture of the two ligands, and used to investigate interactions with bovine serum albumin (BSA). Fluorescence titrations were conducted to determine binding affinity and it was found that the binding constants (Ka) for MHA, MEEE, and mixed-ligand AuNPs were 0.47 ± 0.02 nM-1, 0.40 ± 0.02 nM-1, and 0.48 ± 0.02 nM-1, respectively, indicating that the affinity of BSA for both MHA-capped and mixed-ligand AuNPs is higher than that for MEEE-capped AuNPs. The difference between MHA and MEEE-capped and between mixed-ligand and MEEE-capped AuNPs was statistically significant, whereas the difference between the mixed-ligand and MHA-capped AuNPs was not. Fluorescence studies were also used to determine the Hill coefficient n for the binding of BSA with each AuNP type. In all cases n was greater than 1, indicating cooperative binding of BSA molecules to the AuNP surface.

College of the Sciences Presentation Award Winner.

https://digitalcommons.cwu.edu/source/2022/COTS/47