Abstract：
The whey protein β-lactoglobulin (βLG) forms fibrils similar to the amyloid fibrils in the neurodegenerative diseases due to its higher predisposition of β-sheets. This study shed light on the understanding different inorganic Keggin polyoxometalates (POMs) interaction with the protein βLG fibrils. POMs such as Phosphomolybdic acid (PMA), silicomolybdic acid (SMA), tungstosilicic acid (TSA), and phosphotungstic acid (PTA) were used due to their inherent higher anionic charges. The interaction studies were monitored with fluorescence spectra and Thioflavin T assay for both the βLG monomers and the fibrils initially to elucidate the binding ability of the POMs. The binding of POMs and βLG is also demonstrated by molecular docking studies. Zeta potential studies showed the electrostatic mediated higher interactions of the POMs with the protein fibrils. Isothermal titration calorimetry (ITC) studies showed that the molybdenum containing POMs have higher affinity to the protein fibrils than the tungsten. This study could help understanding formation of food grade protein fibrils which have profound importance in food industries.
摘要：
乳清蛋白β-乳球蛋白（βLG）在神经退行性疾病中形成与淀粉样原纤维相似的原纤维，因为它具有较高的β-折叠倾向。这项研究阐明了理解不同的无机Keggin多金属氧酸盐（POM）与蛋白质βLG原纤维的相互作用。POM，如磷钼酸（PMA），硅钼酸(SMA)，钨硅酸（TSA），和磷钨酸（PTA）由于其固有的较高阴离子电荷而被使用。通过荧光光谱和硫黄素T测定监测βLG单体和原纤维的相互作用研究，以初步阐明POM的结合能力。POM和βLG的结合也通过分子对接研究得到证实。Zeta电位研究表明，静电介导的POM与蛋白质原纤维的相互作用更高。等温滴定量热法（ITC）研究表明，含钼的POM对蛋白质原纤维的亲和力高于钨。这项研究可以帮助理解食品级蛋白质原纤维的形成，这些原纤维在食品工业中具有深远的意义。
