Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1310368 | Inorganica Chimica Acta | 2007 | 4 Pages |
We report a flexible route to chemically modify the ferritin nanomagnet. Two dye-labeled ferritins (red- and blue-ferritin) have been prepared by covalently coupling the derivatives of the reactive orange 16 and Remazol brilliant blue R, respectively, to the ferritin surface lysine residues. The study of the particles by transmission electron microscopy showed that the native iron core ferritin remains intact after chemical functionalization of the protein shell. Likewise, magnetic measurements showed that the superparamagnetic properties of the iron core are preserved.
Graphical abstractTwo dye-labeled ferritins (red- and blue-ferritin) have been prepared by covalently coupling the reactive orange 16 and Remazol brilliant blue R, respectively, to the protein surface lysine residues. TEM and magnetic studies indicate that the native iron core ferritin remains intact after chemical functionalization of the protein shell.Figure optionsDownload full-size imageDownload as PowerPoint slide