Nonmonotonic Superparamagnetic Behavior of the Ferritin Iron Core Revealed via Quantum Spin Relaxometry.

Ferritin is the primary storage protein in our body and is of significant interest in biochemistry, nanotechnology, and condensed matter physics. More specifically within this sphere of interest are the magnetic properties of the iron core of ferritin, which have been utilized as a contrast agent in applications such as magnetic resonance imaging. This magnetism depends on both the number of iron atoms present, L , and the nature of the magnetic ordering of their electron spins. In this work, we create a series of ferritin samples containing homogeneous iron loads and apply diamond-based quantum spin relaxometry to systematically study their room temperature magnetic properties. We observe anomalous magnetic behavior that can be explained using a theoretical model detailing a morphological change to the iron core occurring at relatively low iron loads. This model provides an L 0.35±0.06 scaling of the uncompensated Fe spins, in agreement with previous theoretical predictions. The necessary inclusion of this morphological change within the model is also supported by electron microscopy studies of ferritin with low iron content. This provides evidence for a magnetic consequence of this morphological change and positions diamond-based quantum spin relaxometry as an effective, noninvasive tool for probing the magnetic properties of metalloproteins. The low detection limit (ferritin 2% loaded at a concentration of 7.5 ± 0.4 μg/mL) also makes this a promising method for precision applications where low analyte concentrations are unavoidable, such as in biological research or even clinical analysis.