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Number of results
2012 | 121 | 5-6 | 1305-1307

Article title

Presence of Magnetic Fluids Leads to the Inhibition of Insulin Amyloid Aggregation

Content

Title variants

Languages of publication

EN

Abstracts

EN
Insulin amyloid aggregation caused serious problems in the treatment of diabetes by insulin injection or by insulin pumps. In vitro formation of insulin amyloid fibrils was investigated in presence of several types of magnetic fluids. Interaction of magnetic fluids with insulin amyloid aggregates led to decrease of insulin fibrillization. The inhibiting activities are affected by coating layer of studied magnetic fluids as well as by their physical properties (diameter, concentration of magnetic particles). The highest inhibiting efficiencies were detected for sterically stabilized magnetic fluids in saline solution (75%) and for magnetic fluids modified by dextran (80%).

Keywords

EN

Contributors

author
  • Institute of Experimental Physics, Slovak Academy of Sciences, Kosice, Slovakia
author
  • Institute of Experimental Physics, Slovak Academy of Sciences, Kosice, Slovakia
  • Department of Biochemistry, Faculty of Science, Safarik University, Kosice, Slovakia
author
  • Institute of Experimental Physics, Slovak Academy of Sciences, Kosice, Slovakia
author
  • Institute of Experimental Physics, Slovak Academy of Sciences, Kosice, Slovakia
author
  • Institute of Experimental Physics, Slovak Academy of Sciences, Kosice, Slovakia
  • Institute of Experimental Physics, Slovak Academy of Sciences, Kosice, Slovakia
author
  • Institute of Experimental Physics, Slovak Academy of Sciences, Kosice, Slovakia
author
  • Institute of Experimental Physics, Slovak Academy of Sciences, Kosice, Slovakia
  • Institute of Experimental Physics, Slovak Academy of Sciences, Kosice, Slovakia
author
  • Institute of Biology and Ecology, Faculty of Science, Safarik University, Kosice, Slovakia
author
  • Institute of Experimental Physics, Slovak Academy of Sciences, Kosice, Slovakia

References

  • 1. J.D. Sipe, Amyloid Proteins, Wiley-VCH, Weinheim 2005
  • 2. D.M. Walsh, D.J. Selkoe, Protein Pept. Lett. 11, 213 (2004)
  • 3. S.S.-S. Wang, K.-N. Liu, T.-C. Han, Biochim. Biophys. Acta Mol. Basis Dis. 1802, 519 (2010)
  • 4. M. Kanapathipillai, S.H. Ku, K. Girigoswami, Ch.B. Park, Biochem. Biophys. Res. Com. 365, 808 (2008)
  • 5. A. Bellova, E. Bystrenova, M. Koneracka, P. Kopcansky, F. Valle, M. Timko, J. Bagelova, F. Biscarini, Z. Gazova, Nanotechnology 21, 065103 (2010)

Document Type

Publication order reference

Identifiers

YADDA identifier

bwmeta1.element.bwnjournal-article-appv121n5-6p98kz
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