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ORCID
https://orcid.org/0000-0002-7020-598X
Access Type
Campus-Only Access for Five (5) Years
Document Type
thesis
Degree Program
Food Science
Degree Type
Master of Science (M.S.)
Year Degree Awarded
2019
Month Degree Awarded
May
Abstract
Over the past decades, numerous studies shown curcumin, a dietary compound derived from turmeric, has a variety of health-promoting actions, such as anti-oxidant, anti-microbial, anti-inflammatory, and anti-cancer effects, making curcumin the most promising dietary compound for disease prevention. However, the underlying mechanisms by which curcumin has these health-promoting effects are not well understood. A better understanding of the molecular mechanism of curcumin could help to develop novel strategies to reduce the risks of some human diseases.
Protein thiols play important roles in cell signaling, and recent studies showed that curcumin could covalently react with protein thiols, supporting that curcumin-protein interactions could contribute to the health-promoting effects of curcumin. However, the curcumin-protein interactions are under-studied. Notably, it remains unknown whether oral intake of curcumin could covalently interact with protein in vivo. In this project, we synthesized a click chemistry probe of curcumin (Di-Cur), and used this probe to characterize curcumin-protein interactions both in vitro and in vivo using a click chemistry-based imaging approach. Our results demonstrate that orally administrated curcumin could form curcumin-protein adducts in specific tissues of the mice, which may contribute to the potent biological effects and poor pharmacokinetics of curcumin.
DOI
https://doi.org/10.7275/14188070
First Advisor
Guodong Zhang
Recommended Citation
Zhou, Jingyi, "Click Chemistry Approach to Analyze Curcumin-Protein Interactions in vitro and in vivo" (2019). Masters Theses. 810.
https://doi.org/10.7275/14188070
https://scholarworks.umass.edu/masters_theses_2/810