The 57 Fe hyperfine interactions in human liver ferritin and its iron-polymaltose analogues: the heterogeneous iron core
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The 57 Fe hyperfine interactions in human liver ferritin and its iron-polymaltose analogues: the heterogeneous iron core model M. I. Oshtrakh1,2 · I. V. Alenkina1,2 · V. A. Semionkin1,2
© Springer International Publishing Switzerland 2016
Abstract Human liver ferritin and its iron-polymaltose pharmaceutical analogues Ferrum Lek, Maltofer® and Ferrifol® were studied using M¨ossbauer spectroscopy at 295 and 90 K. The M¨ossbauer spectra were fitted on the basis of a new model of heterogeneous iron core structure using five quadrupole doublets. These components were related to the corresponding more or less close-packed iron core layers/regions demonstrating some variations in the 57 Fe hyperfine parameters for the studied samples. Keywords M¨ossbauer spectroscopy · Hyperfine interactions · Ferritin · Iron-polymaltose complexes · Iron core
1 Introduction Ferritin molecules are responsible for the iron storage in the body. Mammalian ferritin consists of a 24-subunits protein shell with a size of ∼12 nm and a cavity inside the shell with a diameter of ∼8 nm (for review of ferritin structure and functions see, for instance, [1–4]). The cavity contains a nanosized iron core in the form of ferrihydrite (5Fe2 O3 ×9H2 O) or ferric hydrous oxide complex with some inorganic phosphates with an approximate formula (FeOOH)8 (FeO:OPO3 H2 ). The largest amount of iron atoms may be up to 4500, however,
This article is part of the Topical Collection on Proceedings of the International Conference on Hyperfine Interactions and their Applications (HYPERFINE 2016), Leuven, Belgium, 3–8 July 2016 M. I. Oshtrakh
[email protected] 1
Department of Physical Techniques and Devices for Quality Control, Institute of Physics and Technology, Ural Federal University, Ekaterinburg 620002, Russian Federation
2
Department of Experimental Physics, Institute of Physics and Technology, Ural Federal University, Ekaterinburg 620002, Russian Federation
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normal mammalian ferritin core contains of about 2500 iron atoms. The structure of ferritin iron core is a subject of numerous studies some of which have been discussed briefly in [5, 6] (see references therein). The core structure was considered as being in crystalline and amorphous forms, as monocrystalline or polycrystalline forms or consists of a mixture of these structures, as one crystallite, several crystallites, multidomain and polyphasic iron core, and so on. Basing on these structures different iron core models were used to fit the ferritin M¨ossbauer spectra. For instance, the core-shell model was used in [7, 8] to fit spectra using two components, the polyphasic model was considered in [9, 10] with three spectral components. Some ferritin analogues are used and developed as medicaments for treatment the iron deficiency anemia. These analogues consist of a polysaccharide shell surrounding the nanosized iron core in the form of akagan´eite (β-FeOOH). The structure of the iron core in ferritin analogues is also unclear. For instance, in
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