<br/>Engineered nanomaterials (ENMs) support the growth of new and competitive technologies in the fields of energy production and biomedical science. While tens thousand tons of ENMs are produced annually, their health effects remain uncertain, calling for interdisciplinary research to assess the biological impacts from ENMs and discover the fundamental factors that contribute to such impacts. My research group actively develops analytical tools to elucidate the complex interaction among ENMs, biomolecules, and biological systems. Our focus is on the biomolecular layer, i.e. biocorona, formed on ENMs present in biofluids. The physicochemical properties of ENMs strongly affect the formation of the biocorona, which subsequently mediates the interaction between ENMs and the biological system. On the other hand, the molecular structure of a protein could be altered when attached to ENMs, affecting their performance present in biological systems. To understand such impacts better, we developed a method that relies on limited proteolysis coupled with LC-MS/MS to reveal the changes in protein structure when it binds to ENM. Adsorption of proteins, transferrin and catalase, on the polystyrene (PS) or iron oxide (IO) NPs was analyzed with this method. Both increased and decreased proteolytic efficiency in certain regions on the proteins were observed. Identification of the peptides affected by protein-NP interaction led to proper prediction of the outcomes to protein function as well as to NP colloidal stability, demonstrating the utility of this method in helping to elucidate the potential biological outcomes of the protein-NP conjugate. Overall, the present work has demonstrated that limited proteolysis is a valuable tool for improving the rational design of the protein conjugated NPs for biomedical applications, and for better understanding of the biological behaviors of the engineered NPs.<br/>

Protein conformational change induced by nanomaterials elucidated with limited proteolysis

2019 Fall National Meeting

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