Anomalous Mössbauer line broadening for nanosized hydrous ferric oxide cores in ferritin and its pharmaceutical analogue Ferrum Lek in the temperature range 295–90 K
Source abstract
Abstract
Mossbauer spectra of ferritin and its pharmaceutical analogue Ferrum Lek, both containing nanosized hydrous ferric oxides cores in the forms of ferrihydrite and akaganeite, respectively, were measured in the temperature range 295–90 K. An anomalous line broadening with temperature decrease was observed for ferritin below ~150 K and for Ferrum Lek below ~130 K. Some anomalies were also observed below these temperatures for spectral area and quadrupole splitting.
Source: openaire · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Iron oxide chemistry and applications · Iron Metabolism and Disorders · Magnetic Properties and Synthesis of Ferrites
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References (23)
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1. Aisen P, Listowsky I (1980) Iron transport and storage proteins. Ann Rev Biochem 49:357–39310.1146/annurev.bi.49.070180.002041 ↗
2. Alenkina IV, Oshtrakh MI, Klepova YuV, Dubiel SM, Sadovnikov NV, Semionkin VA (2013a) Comparative study of the iron cores in human liver ferritin, its pharmaceutical models and ferritin in chicken liver and spleen tissues using Mössbauer spectroscopy with a high velocity resolution. Spectrochim Acta A 100:88–9310.1016/j.saa.2012.02.083 ↗
3. Alenkina IV, Oshtrakh MI, Semionkin VA, Kuzmann E (2013b) Comparative study of nanosized iron cores in human liver ferritin and its pharmaceutically important models Maltofer® and Ferrum Lek using Mössbauer spectroscopy. Bull Rus Acad Sci Phys 77:739–74410.3103/S1062873813060038 ↗
4. Bauminger ER, Harrison PM (2003) Ferritin, the path of iron into the core, as seen by Mössbauer spectroscopy. Hyperfine Interact 151(152):3–1910.1023/B:HYPE.0000020401.01552.56 ↗
5. Bauminger ER, Nowik I, Harrison PM, Treffry A (1987) First-order phase transition in protein dynamics of ferritin. Hyperfine Interact 33:241–24810.1007/BF02394112 ↗
6. Bonville P, Gilles C (2001) Search for incoherent tunnel fluctuations of the magnetization in nanoparticles of artificial ferritin. Phys B 304:237–24510.1016/S0921-4526(01)00540-3 ↗
7. Chua-anusorn W, Mun H-R, Webb J, Gorham NT, St. Pierre TG (2002) Effect of precipitation temperature and number of iron atoms per molecule on the structure of hydrated iron(III) oxyhydroxide ferritin cores synthesised in vitro. Hyperfine Interact 144(145):279–28810.1023/A:1025494830924 ↗
8. Funk F, Long GJ, Hautot D, Büchi R, Christl I, Weidler PG (2001) Physical and chemical characterization of therapeutic iron containing materials: a study of several superparamagnetic drug formulations with the β-FeOOH or ferrihydrite structure. Hyperfine Interact 136:73–9510.1023/A:1015552311359 ↗
9. Harrison PM, Arosio P (1996) The ferritins: molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta 1275:161–20310.1016/0005-2728(96)00022-9 ↗
10. Heald SM, Stern EA, Bunker B, Holt EM, Holt SL (1979) Structure of the iron-containing core in ferritin by the extended X-ray absorption fine structure technique. J Am Chem Soc 101:67–7310.1021/ja00495a012 ↗
11. Kilcoyne SH, Gorisek A (1998) Magnetic properties of iron dextran. J Magn Magn Mater 177–181:1457–145810.1016/S0304-8853(97)00678-1 ↗
12. Madsen DE, Hansen MF, Bendix J, Mørup S (2008) On the analysis of magnetization and Mössbauer data for ferritin. Nanotechnology 19:31571210.1088/0957-4484/19/31/315712 ↗
13. Mohie-Eldin M-EY, Frankel RB, Gunther L, Papaefthymiou GC (1995) The anomalous Mössbauer fraction of ferritin and polysaccharide iron complex (PIC). Hyperfine Interact 96:111–13810.1007/BF02066277 ↗
14. Mørup S, Dumesic JA, Topsøe H (1980) Magnetic microcrystals. In: Cohen RL (ed) Applications of Mössbauer spectroscopy, vol 2. Academic Press, New York, p 110.1016/B978-0-12-178402-7.50007-5 ↗
15. Oshtrakh MI, Semionkin VA (2013) Mössbauer spectroscopy with a high velocity resolution: advances in biomedical, pharmaceutical, cosmochemical and nanotechnological research. Spectrochim Acta A 100:78–8710.1016/j.saa.2012.03.020 ↗
16. Oshtrakh MI, Semionkin VA, Prokopenko PG, Milder OB, Livshits AB, Kozlov AA (2001) Hyperfine interactions in the iron cores from various pharmaceutically important iron–dextran complexes and human ferritin: a comparative study by Mössbauer spectroscopy. Int J Biol Macromol 29:303–31410.1016/S0141-8130(01)00181-7 ↗
17. Oshtrakh MI, Milder OB, Semionkin VA (2008) Mössbauer spectroscopy with high velocity resolution in the study of ferritin and imferon: preliminary results. Hyperfine Interact 185:39–4610.1007/s10751-008-9809-3 ↗
18. Oshtrakh MI, Semionkin VA, Milder OB, Novikov EG (2009) Mössbauer spectroscopy with high velocity resolution: an increase of analytical possibilities in biomedical research. J Radioanal Nucl Chem 281:63–6710.1007/s10967-009-0079-6 ↗
19. Oshtrakh MI, Alenkina IV, Dubiel SM, Semionkin VA (2011) Structural variations of the iron cores in human liver ferritin and its pharmaceutically important models: a comparative study using Mössbauer spectroscopy with a high velocity resolution. J Mol Struct 993:287–29110.1016/j.molstruc.2010.10.045 ↗
20. Papaefthymiou GC (2009) Nanoparticle magnetism. Nano Today 4:438–44710.1016/j.nantod.2009.08.006 ↗
21. Papaefthymiou GC (2010) The Mössbauer and magnetic properties of ferritin cores. Biochim Biophys Acta 1800:886–89710.1016/j.bbagen.2010.03.018 ↗
22. Semionkin VA, Oshtrakh MI, Milder OB, Novikov EG (2010) A high velocity resolution Mössbauer spectrometric system for biomedical research. Bull Rus Acad Sci Phys 74:416–42010.3103/S1062873810030287 ↗
23. Theil EC (1987) Ferritin: structure, gene regulation, and cellular function in animals, plants, and microorganisms. Ann Rev Biochem 56:289–31510.1146/annurev.bi.56.070187.001445 ↗