Construction of thermally robust and porous shrimp ferritin crystalline for molecular encapsulation through intermolecular arginine-arginine attractions
Construction of thermally robust and porous shrimp ferritin crystalline for molecular encapsulation through intermolecular arginine-arginine attractions
复制标题
通过分子间精氨酸-精氨酸吸引力构建耐热多孔虾铁蛋白晶体以进行分子封装
DOI：
10.1016/j.foodchem.2021.129089
复制
发表时间：
2021-02-03
期刊：
影响因子：
8.8
通讯作者：
Zhao, Guanghua
中科院分区：
文献类型：
--
作者：
Chen, Hai;Zhang, Tuo;Zhao, Guanghua
Protein colloid crystals are considered as high porous soft materials, presenting great potentials in nutrients and drug encapsulation, but protein crystal fabrication usually needs precipitant and high protein concentration. Herein, an easy implemented approach was reported for the construction of protein colloid crystals in diluted solution with shimp ferritin as building blocks by taking advantage of the strength of multiple intermolecular arginine-arginine interactions. The X-ray single-crystal structure reveals that a group of exquisite argininearginine interactions between two neighboring ferritin enable them self-assembly into long-range ordered protein soft materials. The arginine-arginine interactions mediate crystal generation favored at pH 9.5 with 200 mM NaCl, and the resulting colloid crystals exhibit high thermal stability (90 degrees C for 30 min). Importantly, the interglobular cavity in colloid crystals is three times larger in volume than that of intrinsic ferritin cavity in each unit cell, which can be used for molecular encapsulation.
