Reconstituted Super Paramagnetic Protein "Magnetotransferrin" for Brain Targeting to Attenuate Parkinsonism

Transferrin is an iron transporting protein consisting of bilobal protein shells (apotransferrin) with dual domains in each lobe, holding an interdomain iron binding cleft. This cleft is useful in synthesizing an iron oxide core inside the transferrin shell. In vitro reconstitution chemistry provides a nano-dimensional synthesis of the mineral core inside the protein shell. The present study demonstrates the synthesis of magnetotransferrin with reconstitution of apotransferrin to form iron oxide nanoparticles within the transferrin. Transmission electron microscopy investigations along with analysis of electronic diffraction patterns and magnetometry studies indicate entrapment of superparamagnetic iron (III) oxide nanoparticles. In vivo/ex vivo imaging of the brain and immunogold staining of brain sections further validate the brain targeting potential of "magnetotransferrin". The in vivo therapeutic potential of magneto transferrin has been demonstrated by induction of TRPV1 magnetic stimuli protein, having an important regulatory role in Parkinsonism management. In an exploration of neuroprotective mechanisms, deacetylation of H3K27 of synuclein has been revealed through the TRPV1-mediated HDAC3 activation in the treatment of Parkinsonism. Thus, this magnetic protein could be a potent candidate for brain targeting, bio-imaging, and therapy of neurological infirmities.