Understanding the three way interactions between serum albumin, copper, and epigallocatechin gallate can provide insight into how biological systems deal with excess copper, as well as the potential benefit of the major polyphenol in green tea, epigallocatechin gallate. The redox chemistry of copper plays a critical role in biological systems, as it is very useful in electron transfer mechanisms, but an excess of copper, which can bind to the protein serum albumin, can also be toxic to these same systems. Epigallocatechin gallate (EGCg), which can also bind to serum albumin, is the major polyphenolic compound in green tea, and it has been suggested that it is able to treat chronic diseases. The different interactions between EGCg, BSA, and Cu(II) were analyzed using UV-Vis spectrophotometry. Adding EGCg to BSA-Cu complexes was found to not impact copper bound to BSA with high affinity, but does change the state of the bound copper with low affinity. The addition of EGCg to BSA and copper complexes results in the formation of a new peak at 475 nm. The new peak that forms cannot be attributed to the formation of EGCg-Cu complexes or BSA-EGCg complexes, suggesting that there is a new complex that forms between the three species when mixed.
Author: Anne K. Cunagin
Faculty Advisor: Ann E. Hagerman, Department of Chemistry and Biochemistry
Graduate Student Advisor: Meiling Fu, Department of Chemistry and Biochemistry
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