Key Laboratory of Food Nutrition and Safety of SDNU, Provincial Key Laboratory of Animal Resistant Biology, College of Life Science, Shandong Normal University, Jinan 250014, China.
Molecules. 2019 Aug 31;24(17):3171. doi: 10.3390/molecules24173171.
Theaflavin is a kind of multi-pharmacological and health beneficial black tea factor. The aim of this study is to investigate the mechanisms by which theaflavin interacts with glycosylated and non-glycosylated serum albumins and compares their binding properties. Fluorescence and ultraviolet spectra indicated that theaflavin interacted with native and glycated human serum albumin through a static quenching mechanism and had a higher degree of quenching of human serum albumin. The thermodynamic parameters revealed that the combinations of theaflavin with native and glycated human serum albumin were a spontaneous endothermic reaction, and the hydrophobic force was a major driving force in the interaction process. Zeta potential, particle size, synchronous fluorescence, three-dimensional fluorescence spectroscopy and circular dichroism further clarified the effect of theaflavin on the conformation of human serum albumin structure were more pronounced. In addition, site competition experiments and molecular docking technique confirmed that the binding sites of theaflavin on both native and glycated human serum albumin were bound at site II. This study had investigated the effects of glycation on the binding of HSA with polyphenols and the potential nutriology significance of these effects.
茶黄素是一种具有多种药理作用和健康益处的红茶因子。本研究旨在探讨茶黄素与糖化和非糖化血清白蛋白相互作用的机制，并比较它们的结合特性。荧光和紫外光谱表明，茶黄素通过静态猝灭机制与天然和糖化人血清白蛋白相互作用，并且对人血清白蛋白的猝灭程度更高。热力学参数表明，茶黄素与天然和糖化人血清白蛋白的结合是一个自发的吸热反应，疏水作用力是相互作用过程中的主要驱动力。Zeta 电位、粒径、同步荧光、三维荧光光谱和圆二色性进一步阐明了茶黄素对人血清白蛋白结构构象的影响更为明显。此外，位点竞争实验和分子对接技术证实，茶黄素在天然和糖化人血清白蛋白上的结合位点均结合在 II 位点上。本研究探讨了糖化对 HSA 与多酚结合的影响，以及这些影响的潜在营养学意义。
