2 research outputs found
New Interface for Purification of Proteins: One-Dimensional TiO<sub>2</sub> Nanotubes Decorated by Fe<sub>3</sub>O<sub>4</sub> Nanoparticles
In this work, a high
surface area interface, based on anodic one-dimensional (1D) TiO<sub>2</sub> nanotubes homogeneously decorated by Fe<sub>3</sub>O<sub>4</sub> nanoparticles (TiO<sub>2</sub>NTs@Fe<sub>3</sub>O<sub>4</sub>NPs) is reported for the first time for an unprecedented purification
of His-tagged recombinant proteins. Excellent purification results
were achieved from the model protein mixture, as well as from the
whole cell lysate (with His-tagged ubiquitin). Compared to a conventional
immobilized-metal affinity chromatography (IMAC) system, specific
isolation of selected His-tagged proteins on behalf of other proteins
was significantly enhanced on TiO<sub>2</sub>NTs@Fe<sub>3</sub>O<sub>4</sub>NPs interface under optimized binding and elution conditions.
The combination of specific isolation properties, magnetic features,
biocompatibility, and ease of preparation of this material consisting
of two basic metal oxides makes it a suitable candidate for future
purification of recombinant proteins in biotechnology. The principally
new material bears a large potential to open new pathways for discoveries
in nanobiotechnology and nanomedicine