化学
原花青素
聚合度
联动装置(软件)
聚合
生物化学
动作(物理)
食品科学
学位(音乐)
立体化学
作用机理
生物物理学
蛋白质-蛋白质相互作用
作者
YJ Li,Chibuike C. Udenigwe,Carine Le Bourvellec,Lei Zhao,Kai Wang,Zhuoyan Hu,Xuwei Liu
标识
DOI:10.1021/acs.jafc.5c17962
摘要
a = 283.7 L/mol) with LcTLP. Thermodynamic parameters indicated hydrogen bonding as dominant, reflecting an enthalpy-driven process. In RAW264.7 cells, PAPC more effectively suppressed LcTLP-induced NO, TNF-α, and IL-6 secretion by coating LcTLP surface. However, oligomeric proanthocyanidins occupied LcTLP active site by binding to the key residues, including GLU84 and TYR85.
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