Defense Date

2026

Document Type

Thesis

Degree Name

Master of Science

Department

Chemical and Life Science Engineering

First Advisor

Leah Spangler

Abstract

De novo proteins are structurally distinct from proteins found in nature and thus capable of having their amino acid sequence modified to accomplish tasks such as increasing protein-nanoparticle binding without unfolding or decomposing. Zinc Oxide nanoparticles are functionally distinct from their bulk counterparts and are widely used as semiconductors in a variety of fields such as medicine and agriculture. With demand for these nanoparticles increasing, environmentally sustainable methods of Zinc Oxide nanoparticle synthesis are being investigated as an eco-friendly alternative to currently utilized but environmentally hazardous chemical and physical techniques. This research investigates the binding characteristics between Zinc Oxide nanoparticles and various unique de novo proteins. Four proteins underwent transformation, overexpression, and purification before their binding to Zinc Oxide nanoparticles was examined via centrifugation and Biolayer Interferometry analysis. Many key variables involved with Biolayer Interferometry were optimized through a variety of tests to assist in accurately determining binding. The protein containing the most Histidine residues qualitatively showed the greatest binding to the nanoparticles, with the other proteins binding to Zinc Oxide less vigorously. Determining rigorous equilibrium binding affinity values of these proteins was attempted but not fully solved due to exceeding the capabilities of the analysis software. Future endeavors into this research will include the creation of an expanded protein library, the formation of a novel machine learning model to further optimize protein sequences for binding, and the nucleation of Zinc Oxide nanoparticles through protein nucleation.

Rights

© The Author

Is Part Of

VCU University Archives

Is Part Of

VCU Theses and Dissertations

Date of Submission

4-6-2026

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