Layered inorganic/enzyme nanohybrids with selectivity and structural stability upon interacting with biomolecules
Layered inorganic/enzyme nanohybrids with selectivity and structural stability upon interacting with biomolecules
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DOI：
10.1021/bc700224q
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发表时间：
2008-01-01
影响因子：
4.7
通讯作者：
Chiu, Hsin-Cheng
中科院分区：
文献类型：
--
作者：
Chen, Guo-Jing;Yen, Ming-Cheng;Chiu, Hsin-Cheng
通过简单的空间扩大和交换过程，可以实现蛋白质分子在蒙脱石廊道内的有效嵌入，同时保留客体蛋白质的天然构象和生物惰性宿主板的多层结构。容纳蛋白质分子在廊道中的能力可以明显大于由蛋白质分子在颗粒外表面上的朗缪尔型吸附所支配的能力。当蛋白质嵌入程度增加到临界点时，粘土多层结构中的基底间距突然增大。超过这个临界点，纳米杂化物在水解小底物时显示出良好的催化活性，同时建立了与大生物大分子相互作用的屏障。此外，无机/有机纳米杂化物的结构稳定性得到增强，使得当暴露于其他蛋白质时，既不发生生物分子的交换，也不发生层状粘土颗粒的剥离。结果表明，通过无机血小板之间的蛋白质物种的良性调节，这种蛋白质功能的纳米级操纵在开发用于蛋白质治疗和组织工程的新的无机/酶纳米杂化物方面非常有用。
Effective intercalation of protein molecules within the galleries of montmorillonites can be achieved via simple space enlarging and exchange processes while retaining the native conformation of the guest protein and the multilayered structure of the bioinert host plates. The capacity of accommodating protein molecules in the galleries can be markedly larger than that governed by the Langmuir-type adsorption of protein molecules on the external surfaces of particles. The basal spacing in the multilayered structure of clay is abruptly enlarged when the extent of protein intercalation increases to a critical point. Beyond this critical point, the nanohybrids show well-preserved catalytic activity in hydrolyzing small substrates while establishing a barrier to interactions with large biomacromolecules. Furthermore, the structural stability of the inorganic/organic nanohybrids is enhanced such that neither exchange of biomolecules nor exfoliation of layered clay particles occurs when exposed to other proteins. The results indicate that, through the benign accommodation of protein species between the inorganic platelets, this nanoscaled manipulation of protein functions can be highly useful in developing new inorganic/enzyme nanohybrids for protein therapeutics and tissue engineering.