Skip to main content
SpringerLink
Log in

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

  • Research Paper
  • Published:
Journal of Nanoparticle Research Aims and scope Submit manuscript

Abstract

Mössbauer spectra of ferritin and its pharmaceutical analogue Ferrum Lek, both containing nanosized hydrous ferric oxides cores in the forms of ferrihydrite and akaganéite, 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.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6
Fig. 7

Similar content being viewed by others

References

  • Aisen P, Listowsky I (1980) Iron transport and storage proteins. Ann Rev Biochem 49:357–393

    Article  Google Scholar 

  • 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 100:88–93

    Article  Google Scholar 

  • 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 77:739–744

    Article  Google Scholar 

  • Bauminger ER, Harrison PM (2003) Ferritin, the path of iron into the core, as seen by Mössbauer spectroscopy. Hyperfine Interact 151(152):3–19

    Article  Google Scholar 

  • Bauminger ER, Nowik I, Harrison PM, Treffry A (1987) First-order phase transition in protein dynamics of ferritin. Hyperfine Interact 33:241–248

    Article  Google Scholar 

  • Bonville P, Gilles C (2001) Search for incoherent tunnel fluctuations of the magnetization in nanoparticles of artificial ferritin. Phys B 304:237–245

    Article  Google Scholar 

  • 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):279–288

    Article  Google Scholar 

  • 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 136:73–95

    Article  Google Scholar 

  • Harrison PM, Arosio P (1996) The ferritins: molecular properties, iron storage function and cellular regulation. Biochim Biophys Acta 1275:161–203

    Article  Google Scholar 

  • 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 101:67–73

    Article  Google Scholar 

  • Kilcoyne SH, Gorisek A (1998) Magnetic properties of iron dextran. J Magn Magn Mater 177–181:1457–1458

    Article  Google Scholar 

  • Madsen DE, Hansen MF, Bendix J, Mørup S (2008) On the analysis of magnetization and Mössbauer data for ferritin. Nanotechnology 19:315712

    Article  Google Scholar 

  • Mohie-Eldin M-EY, Frankel RB, Gunther L, Papaefthymiou GC (1995) The anomalous Mössbauer fraction of ferritin and polysaccharide iron complex (PIC). Hyperfine Interact 96:111–138

    Article  Google Scholar 

  • Mørup S, Dumesic JA, Topsøe H (1980) Magnetic microcrystals. In: Cohen RL (ed) Applications of Mössbauer spectroscopy, vol 2. Academic Press, New York, p 1

    Chapter  Google Scholar 

  • Oshtrakh MI, Semionkin VA (2013) Mössbauer spectroscopy with a high velocity resolution: advances in biomedical, pharmaceutical, cosmochemical and nanotechnological research. Spectrochim Acta A 100:78–87

    Article  Google Scholar 

  • 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 29:303–314

    Article  Google Scholar 

  • Oshtrakh MI, Milder OB, Semionkin VA (2008) Mössbauer spectroscopy with high velocity resolution in the study of ferritin and imferon: preliminary results. Hyperfine Interact 185:39–46

    Article  Google Scholar 

  • 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 281:63–67

    Article  Google Scholar 

  • 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 993:287–291

    Article  Google Scholar 

  • Papaefthymiou GC (2009) Nanoparticle magnetism. Nano Today 4:438–447

    Article  Google Scholar 

  • Papaefthymiou GC (2010) The Mössbauer and magnetic properties of ferritin cores. Biochim Biophys Acta 1800:886–897

    Article  Google Scholar 

  • Semionkin VA, Oshtrakh MI, Milder OB, Novikov EG (2010) A high velocity resolution Mössbauer spectrometric system for biomedical research. Bull Rus Acad Sci Phys 74:416–420

    Article  Google Scholar 

  • Theil EC (1987) Ferritin: structure, gene regulation, and cellular function in animals, plants, and microorganisms. Ann Rev Biochem 56:289–315

    Article  Google Scholar 

Download references

Acknowledgments

The authors wish to thank Prof. P.G. Prokopenko (Department of Biochemistry, Russian State Medical University, Moscow) for providing the human liver ferritin and Prof. S.M. Dubiel (Faculty of Physics & Applied Computer Science, AGH University of Science & Technology, Kraków) for providing the Ferrum Lek sample. This work was supported in part by the basic financing from the Ministry of Education and Science of Russian Federation and OTKA No 111692. I.V.A. is supported in part by the Ural Federal University development program for the young scientists’ financial support. This work was carried out within the Agreement of Cooperation between the Ural Federal University (Ekaterinburg) and the Eötvös Loránd University (Budapest).

Author information

Authors and Affiliations

  1. Department of Physical Techniques and Devices for Quality Control, Institute of Physics and Technology, Ural Federal University, Yekaterinburg, 620002, Russian Federation

    M. I. Oshtrakh, I. V. Alenkina & V. A. Semionkin

  2. Department of Experimental Physics, Institute of Physics and Technology, Ural Federal University, Yekaterinburg, 620002, Russian Federation

    M. I. Oshtrakh, I. V. Alenkina & V. A. Semionkin

  3. Institute of Chemistry, Eötvös Loránd University, Pázmány sétány1/A., Budapest, 1117, Hungary

    E. Kuzmann

  4. Institute of Molecular Pharmacology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Pusztaszeri út 59-67, Budapest, 1025, Hungary

    Z. Klencsár

Authors
  1. M. I. Oshtrakh
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. I. V. Alenkina
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. E. Kuzmann
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Z. Klencsár
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. V. A. Semionkin
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to M. I. Oshtrakh.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Oshtrakh, M.I., Alenkina, I.V., Kuzmann, E. et al. 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. J Nanopart Res 16, 2363 (2014). https://doi.org/10.1007/s11051-014-2363-9

Download citation

  • Received:

  • Accepted:

  • Published:

  • DOI: https://doi.org/10.1007/s11051-014-2363-9

Keywords

Search

Navigation