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Updated: Aug 16, 2025

Using Magnetometry to Monitor Cellular Incorporation and Subsequent Biodegradation of Chemically Synthetized Iron Oxide Nanoparticles
Published on: February 27, 2021
Interaction and mechanisms in the phosphate-binding of iron(oxyhydr)oxide core-shell nanoparticles
Magdalena Teresa Spicher1, Sebastian Patrick Schwaminger2, Daniela von der Haar-Leistl3
1Fraunhofer Institute for Process Engineering and Packaging (IVV), Giggenhauser Str. 35, 85354 Freising, Germany; Chair of Bioseparation Engineering, School of Engineering and Design, Technical University of Munich, Boltzmannstraße 15, 85748 Garching, Germany.
Hypothesis:
The high binding affinity of iron(oxyhydr)oxides for phosphate has recently been used in medicine to treat hyperphosphatemia, an abnormally elevated phosphate concentration in the blood. For iron(oxyhydr)oxide nanoparticles, the composition of the organic shell has a more significant influence on their interaction with phosphate than is often assumed. This study shows different mechanisms in phosphate binding, using the example of two similar new phosphate-binding agents.
Experiments:
We characterized the phosphate-binding behavior of two iron(oxyhydr)oxide-based nanomaterials with similar composition and particle properties and investigated their binding mechanisms by spectroscopic methods.
Findings:
For the often prescribed Velphoro, we demonstrated a phosphate binding capacity of>210 mg/g. A similar active ingredient named C-PAM binds over 573 mg/g. Spectroscopic measurements highlighted differences in the binding mechanism. While Velphoro binds phosphate via surface complexation independent of pH and adsorbent concentration, C-PAM shows a strong concentration dependence. At low concentrations, phosphate is bound via complexation reactions. The iron(oxyhydr)oxide structure was dissolved at higher phosphate concentrations and formed various iron phosphate species. The substances behave differently upon interaction with phosphate, although being very similar in composition and crystal structure. Thus, we demonstrated a crucial influence of the ligands in the shell on the binding mechanism.
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