作者: Jiang-Lan Yuan , Hui Liu , Xu Kang , Zhong Lv , Guo-Lin Zou
DOI: 10.1016/J.MOLSTRUC.2008.04.017
关键词: Hemoglobin 、 Quenching (fluorescence) 、 Chemistry 、 Circular dichroism 、 Förster resonance energy transfer 、 Apigenin 、 Fluorescence spectroscopy 、 Stereochemistry 、 Binding site 、 Protein secondary structure
摘要: Abstract Apigenin (Ap) and genistein (Ge), a couple of isomeric flavonoids with extensive bioactivities, are the most common dietary ingredients. They have been widely investigated due to their potential therapeutic actions for some diseases. In our work, binding characteristics Ap Ge hemoglobin (Hb) were analyzed fluorescence spectroscopy, circular dichroism (CD) UV–vis absorption spectroscopy. The results indicated that caused strong quenching Hb by static mechanism, but efficiency mechanisms different. site n suggested there was single in Ge. synchronous showed microenvironment around Tyr residues had slight trend polarity decreasing, Trp increased adding Ap. Results CD did not changed secondary structure Hb. According theory Forster resonance energy transfer, distance r between 37 Ap/Ge predicted be 3.4 nm 3.32 nm, respectively. affinity toward higher than