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Electrosynthesized MIPs for transferrin: Plastibodies or nano-filters?
Biosensors and Bioelectronics ( IF 12.6 ) Pub Date : 2018-01-09 , DOI: 10.1016/j.bios.2018.01.011
Xiaorong Zhang , Aysu Yarman , Júlia Erdossy , Sagie Katz , Ingo Zebger , Katharina J. Jetzschmann , Zeynep Altintas , Ulla Wollenberger , Róbert E. Gyurcsányi , Frieder W. Scheller

Molecularly imprinted polymer (MIP) nanofilms for transferrin (Trf) have been synthesized on gold surfaces by electro-polymerizing the functional monomer scopoletin in the presence of the protein target or around pre-adsorbed Trf. As determined by atomic force microscopy (AFM) the film thickness was comparable with the molecular dimension of the target. The target (re)binding properties of the electro-synthesized MIP films was evaluated by cyclic voltammetry (CV) and square wave voltammetry (SWV) through the target-binding induced permeability changes of the MIP nanofilms to the ferricyanide redox marker, as well as by surface plasmon resonance (SPR) and surface enhanced infrared absorption spectroscopy (SEIRAS) of the immobilized protein molecules. For Trf a linear concentration dependence in the lower micromolar range and an imprinting factor of ~5 was obtained by SWV and SPR. Furthermore, non-target proteins including the iron-free apo-Trf were discriminated by pronounced size and shape specificity. Whilst it is generally assumed that the rebinding of the target or of cross-reacting proteins exclusively takes place at the polymer here we considered also the interaction of the protein molecules with the underlying gold transducers. We demonstrate by SWV that adsorption of proteins suppresses the signal of the redox marker even at the bare gold surface and by SEIRAS that the treatment of the MIP with proteinase K or NaOH only partially removes the target protein. Therefore, we conclude that when interpreting binding of proteins to directly MIP-covered gold electrodes the interactions between the protein and the gold surface should also be considered.



中文翻译:

用于转铁蛋白的电合成MIP:质粒或纳米过滤器?

通过在蛋白质靶标的存在下或在预吸附的Trf周围进行电聚合功能单体scopoletin,在金表面上合成了用于转铁蛋白(Trf)的分子印迹聚合物(MIP)纳米膜。如通过原子力显微镜(AFM)确定的,膜厚度与靶的分子尺寸相当。通过循环伏安法(CV)和方波伏安法(SWV)通过MIP纳米膜对铁氰化物氧化还原标记物的靶结合诱导的磁导率变化以及循环伏安法(CV)和方波伏安法(SWV)评估了电合成MIP膜的目标(再)结合性能。通过表面等离振子共振(SPR)和表面增强的红外吸收光谱(SEIRAS)对固定的蛋白分子进行分析。对于Trf,通过SWV和SPR获得了较低的微摩尔范围内的线性浓度依赖性和约5的印迹因子。此外,通过显着的大小和形状特异性区分了非靶蛋白,包括无铁的apo-Trf。虽然通常认为靶标或交叉反应蛋白的重新结合仅发生在聚合物上,但在此我们也考虑了蛋白分子与潜在的金转化子的相互作用。我们通过SWV证明,即使在裸露的金表面,蛋白质的吸附也会抑制氧化还原标记的信号;而SEIRAS证明,用蛋白酶K或NaOH处理MIP只能部分去除目标蛋白质。所以,

更新日期:2018-01-09
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