Thermally-induced whey protein isolate-daidzein co-assemblies: Protein-based nanocomplexes as an inhibitor of precipitation/crystallization for hydrophobic drug
Thermally-induced whey protein isolate-daidzein co-assemblies: Protein-based nanocomplexes as an inhibitor of precipitation/crystallization for hydrophobic drug
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热诱导乳清分离蛋白-黄豆苷元共组装体：基于蛋白质的纳米复合物作为疏水性药物沉淀/结晶的抑制剂
DOI：
10.1016/j.foodchem.2018.09.057
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发表时间：
2019-03-01
期刊：
影响因子：
8.8
通讯作者：
Wang, Shaoyun
中科院分区：
文献类型：
--
作者：
Lv, Liang;Fu, Caili;Wang, Shaoyun
大豆苷元递送的一个挑战是如何有效地抑制其在基于脂质的系统中的沉淀/结晶。本文以不同热处理的乳清分离蛋白（WPI）为疏水性药物结晶抑制剂，研究了其与大豆苷元的相互作用机理。结果表明，大豆苷元存在时，WPI发生了聚集，形成了粒径小于300 nm的纳米颗粒。热变性（85 ℃，20 min）提高了大豆苷元的结合亲和力，Ka = 1.165 x 10（4）M-1，比天然蛋白（Ka = 7.285 x 10（3）M-1）高约1.5倍。热力学计算表明，疏水作用是主要的驱动力。所获得的基于蛋白质的纳米复合物有效地抑制大豆苷元结晶，使其溶解度提高至少2倍，并促进稳定性（在4 ℃下稳定至少2个月）。这些研究结果为WPI的应用提供了新的思路，显示了WPI作为结晶抑制剂直接应用于脂质纳米载体系统的巨大潜力。
One challenge for daidzein delivery is how to efficiently suppress its precipitation/crystallization in a lipid-based system. In this work, whey protein isolate (WPI) with different thermal treatment was employed as a hydrophobic drug crystallization depressor and its interaction mechanism with daidzein was studied. The results indicated WPI aggregated to form nanoparticles (below 300 nm) in the presence of daidzein. Thermal denaturing (85 degrees C, 20 min) improved the binding affinity for daidzein with Ka = 1.165 x 10(4) M-1, about 1.5-fold higher than that of the native protein (Ka = 7.285 x 10(3) M-1). Hydrophobic interaction was the major driving forces based on thermodynamic calculation. The as-obtained protein-based nanocomplexes efficiently inhibited daidzein crystallization, enhancing its solubility at least 2-fold with promoted stability (stable at 4 degrees C for at least 2 months). These findings provide new ideas for the application of WPI, showing great potential to be directly used in lipid nanocarrier system as crystallization depressor.