One-pot synthesis of CuFe2O4 magnetic nanocrystal clusters for highly specific separation of histidine-rich proteins

Abstract

This work reports a facile ligand-free method for the rapid and highly specific separation of histidine (His)-rich proteins using CuFe₂O₄ magnetic nanocrystal clusters (MNCs). Monodispersed CuFe₂O₄ MNCs were synthesized via a simple and economical one-pot hydrothermal process. The resulting MNCs were characterized in detail. The measurements indicated that the MNCs exhibited good dispersion, high crystallinity, and superparamagnetic properties. Moreover, the obtained MNCs had a high saturation magnetization (45.1 emu g⁻¹), which was sufficient to accomplish fast and efficient separation with an external magnetic field. The selectivity and binding capacity of CuFe₂O₄ MNCs were evaluated using a His-rich protein (bovine haemoglobin) and other proteins (bovine serum albumin, human serum albumin, myoglobin, lysozyme, cytochrome c and horseradish peroxidase) containing fewer surface-exposed His residues as model samples. The most distinct feature of the CuFe₂O₄ MNCs is the high haemoglobin binding capacity (4475 mg g⁻¹) due to the coordination between copper(II) ions and surface-exposed histidine resides of haemoglobin. In addition, the CuFe₂O₄ MNCs can be successfully employed to selectively bind and remove abundant haemoglobin from human blood samples. The good results demonstrate the potential of CuFe₂O₄ MNCs in the separation of His-rich proteins.