作者: Juan Zhang , Qin Mi , Min Shen
DOI: 10.1016/J.FOODCHEM.2011.09.070
关键词: Biochemistry 、 Binding constant 、 Fluorescence 、 Tyrosine 、 Isomerization 、 Hydrophobic effect 、 Resveratrol 、 Hydrogen bond 、 Resveratrol binding 、 Chemistry
摘要: Abstract Considering important implication of collagen and resveratrol in platelet aggregation cancer metastasis, interaction between them its biological significance were studied. Resveratrol could interact with to form a 1:1 complex binding constant at about 10 5 M −1 . It decreased fluorescence emission intensities tyrosine, improved the formation excimer-like species dityrosine, had no effect on post-translational, chemical, age-related modifications resveratrol/collagen solution. The process was spontaneous an exothermic reaction. Thermodynamic analysis suggests that both hydrophobic hydrogen bonding played key roles course resveratrol–collagen binding. Moreover, synchronous FT-IR results indicate caused decrease polarity around tyrosine residues resulting conformation alteration. Additionally, isomerisation not prevented but stability addition This work might provide more comprehensive understanding anticancer antiplatelet activities as functional food factor.