Theaflavin-3-gallate specifically interacts with phosphatidylcholine, forming a precipitate resistant against the detergent action of bile salt. Issue 3 (4th March 2018)

• Record Type: Journal Article
• Authors: Narai-Kanayama, Asako; Saruwatari, Kosuke; Mori, Natsumi; Nakayama, Tsutomu
• Is Part Of: Bioscience, biotechnology, and biochemistry. Volume 82:Issue 3(2018)
• Page Start: 466
• Page End: 475
• Publication Date: 2018-03-04
• Subjects: Theaflavin -- phosphatidylcholine -- taurocholate -- micelle; ECg: (−)-epicatechin gallate -- EGCg: (−)-epigallocatechin gallate -- PC: phosphatidylcholine -- PE: phosphatidylethanolamine -- PS: phosphatidylserine -- TF: theaflavin; Biotechnology -- Periodicals; Biochemistry -- Periodicals; 660.6
• DOI: 10.1080/09168451.2017.1422967
• Languages: English
• ISSNs: 0916-8451

Abstract

Abstract: Black tea is a highly popular beverage, and its pigments, polymerized catechins such as theaflavins (TFs), are attracting attention due to their beneficial health effects. In this study, to test the inhibitory activities of TFs on the intestinal absorption of cholesterol, we investigated their effects on phosphatidylcholine (PC) vesicles in the absence or presence of a bile salt. (−)-Epicatechin gallate, (−)-epigallocatechin gallate, and TFs formed insoluble complexes with PC vesicles. Galloylated TFs such as TF2A, TF2B, and TF3 precipitated far more than other polyphenols. The subsequent addition of taurocholate redispersed the polyphenol-PC complexes, except that a large amount of TF2A remained insoluble. After incubation with taurocholate-PC micelles, TF2A elevated the turbidity of the micelle solution, providing red sediments. The TF2A-specific effect was dependent on the PC concentration. These results suggest that TF2A interacts with PC and aggregates in a specific manner different from catechins and other TFs. Abstract: : Specific interaction of TF2A with PC vesicles and the effects of subsequent addition of taurocholate.