Razi University, Kermanshah, Islamic Republic of Iran.
IET Nanobiotechnol. 2012 Sep;6(3):102-9. doi: 10.1049/iet-nbt.2011.0042.
The iron storage protein, ferritin, has a cavity of ∼7 nm in diameter in which iron is oxidised and stored as a hydrated oxide core. Electron transfer is known to be an important step in the sequestering of iron by cellular ferritin. The cavity was used as a nanocontainer to grow cobalt nanoparticles. The immobilisation of ferritin on the electrode surface is essential for various bioelectronic applications. A cobaltferritin-immobilised electrode based on self-assembled monolayer (SAM)-modified gold electrode was developed. The cobaltferritin-immobilised SAM-modified electrode was characterised by electrochemical and atomic force microscopy (AFM) techniques. The results indicated that cobaltferritin was selectively immobilised onto succinimidyl alkanedisulfide-modified Au electrode by the covalent interaction between cobaltferritin and the terminal functional groups of the SAMs. The cobaltferritin immobilised modified electrode showed a direct electron transfer reaction between cobaltferritin and the electrode. The electrochemically regulated uptake and release of cobalts for cobaltferritin immobilised on the SAMs were demonstrated. The results obtained in this study indicate that cobaltferritin has potential for a biomaterial in nanoscale synthesis for potential magnetic, catalytic and biomedical-sensing applications.
铁储存蛋白，铁蛋白，具有直径约 7nm 的空腔，其中铁被氧化并作为水合氧化物核心储存。已知电子转移是细胞铁蛋白螯合铁的重要步骤。该空腔被用作纳米容器来生长钴纳米粒子。铁蛋白在电极表面的固定化对于各种生物电子应用至关重要。基于自组装单层 (SAM) 修饰金电极开发了一种钴铁蛋白固定化电极。通过电化学和原子力显微镜 (AFM) 技术对钴铁蛋白固定化 SAM 修饰电极进行了表征。结果表明，通过钴铁蛋白和 SAM 末端官能团之间的共价相互作用，钴铁蛋白选择性地固定在琥珀酰亚胺烷二硫醇修饰的 Au 电极上。钴铁蛋白固定化修饰电极在电极之间表现出钴铁蛋白和电极之间的直接电子转移反应。证明了固定在 SAM 上的钴铁蛋白对钴的电化学调节摄取和释放。本研究的结果表明，钴铁蛋白在纳米尺度合成中具有作为生物材料的潜力，用于潜在的磁性、催化和生物医学传感应用。
