Functionalization of γ-Fe2O3 nanoparticles through the grafting of an organophosphorous ligand
Functionalization of γ-Fe2O3 nanoparticles through the grafting of an organophosphorous ligand
复制标题
DOI：
10.1016/j.snb.2008.05.022
复制
发表时间：
2008-09-25
影响因子：
8.4
通讯作者：
Horner, Olivier
中科院分区：
文献类型：
--
作者：
Georgelin, Thomas;Moreau, Bernard;Horner, Olivier
一种由胺基团封端的有机磷配体首次被用来功能化γ-Fe_2O_3纳米粒子，并以共价方式将一种酶固定在其表面。通过末端氨基参与的还原胺化反应，将β-葡萄糖苷酶固定在磁铁矿纳米颗粒上，结合酶的活性用经典的Michaelis-Menten动力学进行了评价。事实上，结合的酶对底物的亲和力被保存下来，并且不会受到纳米颗粒表面上大量酶的影响。此外，与游离酶相比，相关的酶活性略有下降，这种功能化的纳米粒子可以通过磁场的作用来改善生物分子在生物医学中的传递和回收。它们还可以提供一种磁性载体，可以作为造影剂、生物标记和磁性热疗的介体。(C)2008爱思唯尔B.V.保留所有权利
An organophosphorous ligand terminated by an amine group has been used here for the first time to functionalize gamma-Fe2O3 nanoparticles and to immobilize an enzyme onto their surface in a covalent way. The immobilization of beta-glucosidase onto the maghemite nanoparticles was carried in this work out via a reductive amination reaction pathway which involves the terminal amine group on the ligand.The enzymatic activity of the bound enzyme was evaluated in terms of the classical Michaelis-Menten kinetics. Indeed, the affinity of the bound enzyme for the substrate is preserved and is not affected by the high amount of enzymes onto the surface of the nanoparticles. Moreover, the related enzymatic activity slightly decreases compared to that of the free enzyme.Such functionalized nanoparticles could help to improve the delivery and the recovery of biomolecules in biomedical applications by using a magnetic field. They could also provide a magnetic support which could be involved as a contrast agent, a biological label and a mediator for magnetic hyperthermia. (C) 2008 Elsevier B.V. All rights reserved