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Showing posts with the label EGCG,cancer cells,molecular mechanisms ,p53,tumor suppressor,MDM2, ubiquitination, anti-tumor activity, polyphenolic compounds,tumor suppressor,anti-aging effects,DNA damage

Great Green Tea: Half from West Lake, Half from Thousand Island Lake

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 When people think of China’s finest green tea, they picture West Lake in Hangzhou—the villages of Longjing and Meijiawu, Emperor Qianlong’s legendary “Eighteen Imperial Tea Bushes,” and a cup of flat, jade-green leaves releasing delicate chestnut notes. And they’re not wrong. West Lake Longjing is indeed one of China’s most iconic teas. But few know that 150 kilometers southwest of Hangzhou, amid the emerald waters of Thousand Island Lake, lies another chapter of tea history—one far older, equally profound, and unjustly overlooked. Here, during the Tang Dynasty (618–907 CE), tribute tea known as Jiukeng Maojian was sent to the imperial court. Lu Yu, the Sage of Tea, recorded its origin in his Classic of Tea (Cha Jing). Centuries later, seeds from this very land would travel to Japan, Kenya, and beyond, shaping green tea across continents. Today, protected as a Class-I national water source, this region bans chemical pesticides entirely—yielding tea of unmatched purity and freshnes...

New study finds that EGCG in green tea can inhibit cancer cell growth by interacting with the N-terminal domain of p53.

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  The major polyphenolic compound in  green tea , epigallocatechin-3-gallate (EGCG), has been shown to induce apoptosis in cancer cells, but its  molecular mechanism  is not fully understood. Recently, a team led by  Chunyu Wang  at Rensselaer Polytechnic Institute (with  China Agricultural University  as the first affiliation and Jing Zhao as the first author of the paper) published a research paper in  Nature Communications  titled "EGCG binds intrinsically disordered N-terminal domain of p53 and disrupts p53-MDM2 interaction". Using SPR and  NMR techniques , the study found that EGCG directly interacts with the  tumor suppressor p53 , with the intrinsically disordered N-terminal domain (NTD) identified as the main binding site. Large-scale atomic simulations, SAXS and AUC results showed that the EGCG-NTD interaction is dynamic, and EGCG leads to the appearance of a subset of compact bound conformations. The EGCG-p53 interact...