title: Comparative studies on interactions of baicalein, baicalin and scutellarin with lysozyme.
abstract: The interactions of baicalein, baicalin and scutellarin with lysozyme (LYSO) were studied by fluorescence and UV spectroscopy. The results showed that all the three flavones can quench the fluorescence of LYSO via static quenching with the distance between the donor and acceptor less than 7 nm. The hydroxyl at B-ring gave flavones an advantage to binding with LYSO. Electrostatic forces played a major role in stabilizing baicalein-LYSO complex and baicalin-LYSO complex, whereas hydrophobic interactions in scutellarin-LYSO. Furthermore, the presence of pantothenic acid can increase the binding constant and the number of binding sites between flavones and LYSO.
authors: Pharmacognosy Department, Pharmaceutical College, Hebei Medical University, 361 Zhongshan East Road, Shijiazhuang City, Hebei Province 050017, PR China. hy9317536@126.com
authors: Yun
authors: Y
authors: Huang
authors: Li-Jian
authors: LJ
authors: Cui
authors: Jian-Ming
authors: JM
authors: Wang
authors: Kun
authors: K
authors: Huo
authors: Chen
authors: C
authors: Chen
authors: Wen-Hong
authors: WH
authors: Zhan
authors: Yu-Hong
authors: YH
authors: Dou
mesh_terms: D000818:Animals; D000890:Anti-Infective Agents / Q000494:pharmacology*; D047310:Apigenin / Q000494:pharmacology*; D002645:Chickens; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D044950:Flavanones / Q000494:pharmacology*; D005419:Flavonoids / Q000494:pharmacology*; D005965:Glucuronates / Q000494:pharmacology*; D009113:Muramidase / Q000378:metabolism*; D010205:Pantothenic Acid / Q000494:pharmacology; D011485:Protein Binding; D013050:Spectrometry, Fluorescence
chemical_list: D000890:Anti-Infective Agents; D004791:Enzyme Inhibitors; D044950:Flavanones; D005419:Flavonoids; D005965:Glucuronates; C484876:scutellarin; D010205:Pantothenic Acid; C038044:baicalin; C006680:baicalein; D047310:Apigenin; D009113:Muramidase