TROY, N.Y. (NEWS10) — An antioxidant found in green tea may increase levels of p53, a natural anti-cancer protein, according to Rensselaer Polytechnic Institute (RPI). The p53 protein is also known as the “guardian of the genome” for its ability to repair DNA damage or destroy cancerous cells.
Published on Friday in Nature Communications, a study of the direct interaction between p53 and the green tea compound epigallocatechin gallate (EGCG) points to a new target for cancer drug discovery.
“Both p53 and EGCG molecules are extremely interesting. Mutations in p53 are found in over 50% of human cancer, while EGCG is the major anti-oxidant in green tea, a popular beverage worldwide,” said Chunyu Wang, corresponding author and a professor of biological sciences at Rensselaer Polytechnic Institute. “Now we find that there is a previously unknown, direct interaction between the two, which points to a new path for developing anti-cancer drugs. Our work helps to explain how EGCG is able to boost p53’s anti-cancer activity, opening the door to developing drugs with EGCG-like compounds.”
Wang, a member of the Rensselaer Center for Biotechnology and Interdisciplinary Studies, is an expert in using nuclear magnetic resonance spectroscopy to study specific mechanisms in Alzheimer’s disease and cancer, including p53, which he described as “arguably the most important protein in human cancer.”
RPI says p53 has several well-known anti-cancer functions, including stopping cell growth to allow for DNA repair, activating the repair, and initiating cell death if the DNA damage cannot be repaired. One end of the protein, known as the N-terminal domain, has a flexible shape and can potentially serve several functions depending on its interaction with molecules.
EGCG is a natural antioxidant, which means it helps to undo the damage caused during oxygen metabolism. Found abundantly in green tea, EGCG is also packaged as an herbal supplement.
Wang’s team found that the interaction between EGCG and p53 preserves the protein against degradation. Typically, after being produced within the body, p53 is quickly degraded when the N-terminal domain interacts with a protein called MDM2. This regular cycle of production and degradation holds p53 levels at a low constant.