Andrea Antosova

Publications (4)15.31 Total impact

• Article: Attenuation of the insulin amyloid aggregation in presence of Fe3O4-based magnetic fluids.

  Katarina Siposova, Eva Bystrenova, Andrea Antosova, Martina Koneracka, Vlasta Zavisova, Peter Kopcansky, Zuzana Gazova
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  ABSTRACT: Presence of protein amyloid deposits is associated with pathogenesis of amyloid-related diseases. Insulin amyloid aggregates have been reported in a patient with diabetes undergoing treatment by injection of insulin. We have investigated the interference of insulin amyloid aggregation with two Fe3O4-based magnetic fluids. The magnetic fluids are able to inhibit insulin amyloid fibrillization and promote disassembly of amyloid fibrils. The cytotoxic effect of amyloid fibrils is attenuated in presence of magnetic fluids probably due to reduction of the fibrils. We suggest that present findings propose the potential use of Fe3O4-based magnetic fluids as the therapeutic agents targeting insulin-associating amyloidosis.
  General Physiology and Biophysics 03/2013; · 1.19 Impact Factor
• Article: Binding of Glyco-acridine Derivatives to Lysozyme leads to Inhibition of Amyloid Fibrillization.

  Quan Van Vuong, Katarina Siposova, Trang Truc Nguyen, Andrea Antosova, Lucia Balogova, Ladislav Drajna, Jan Imrich, Mai Suan Li, Zuzana Gazova
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  ABSTRACT: While amyloid-related diseases are at the center of intense research efforts, no real cure is currently being directed toward treating the diseases. The experimental and computational techniques were used to study the ability of glyco-acridines to prevent lysozyme amyloid fibrillization in vitro. Fluorescence spectroscopy and transmission electron microscopy have shown that glyco-acridines inhibit amyloid aggregation of lysozyme; the inhibition efficiency characterized by the half-maximal inhibition concentration IC50 was affected by derivative structure and concentration. We have investigated relationship between the binding affinity and the inhibition activity of the compounds. The good correlation was reached within the framework of the semiempirical quantum PM6-DH+ method pointing to importance of quantum effects in binding of glyco-acridine derivatives to lysozyme. The role of linkers may be understood within the Valence Bond theory. Our data provide a basis for the development of novel small molecules effective in therapy of amyloid-related diseases.
  Biomacromolecules 02/2013; · 5.48 Impact Factor
• Article: Depolymerization of insulin amyloid fibrils by albumin-modified magnetic fluid.

  Katarina Siposova, Martina Kubovcikova, Zuzana Bednarikova, Martina Koneracka, Vlasta Zavisova, Andrea Antosova, Peter Kopcansky, Zuzana Daxnerova, Zuzana Gazova
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  ABSTRACT: Pathogenesis of amyloid-related diseases is associated with the presence of protein amyloid deposits. Insulin amyloids have been reported in a patient with diabetes undergoing treatment by injection of insulin and causes problems in the production and storage of this drug and in pplication of insulin pumps. We have studied the interference of insulin amyloid fibrils with a series of 18 albumin magnetic fluids (MFBSAs) consisting of magnetite nanoparticles modified by different amounts of bovine serum albumin (w/w BSA/Fe₃O₄ from 0.005 up to 15). We have found that MFBSAs are able to destroy amyloid fibrils in vitro. The extent of fibril depolymerization was affected by nanoparticle physical-chemical properties (hydrodynamic diameter, zeta potential and isoelectric point) determined by the BSA amount present in MFBSAs. The most effective were MFBSAs with lower BSA/Fe₃O₄ ratios (from 0.005 to 0.1) characteristic of about 90% depolymerizing activity. For the most active magnetic fluids (ratios 0.01 and 0.02) the DC50 values were determined in the range of low concentrations, indicating their ability to interfere with insulin fibrils at stoichiometric concentrations. We assume that the present findings represent a starting point for the application of the active MFBSAs as therapeutic agents targeting insulin amyloidosis.
  Nanotechnology 02/2012; 23(5):055101. · 3.98 Impact Factor
• Article: Structure-activity relationship of acridine derivatives to amyloid aggregation of lysozyme.

  Andrea Antosova, Beatrice Chelli, Eva Bystrenova, Katarina Siposova, Francesco Valle, Jan Imrich, Maria Vilkova, Pavol Kristian, Fabio Biscarini, Zuzana Gazova
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  ABSTRACT: Amyloid-related diseases (such as Alzheimer's disease or diabetes type II) are associated with self-assembly of protein into amyloid aggregates. Spectroscopic and atomic force microscopy were used to determine the ability of acridines to affect amyloid aggregation of lysozyme. We have studied the effect of acridine derivatives on the amyloid aggregation of lysozyme to investigate the acridine structure-activity relationship. The activity of the effective planar acridines was characterized by the half-maximum depolymerization concentration DC(50) and half-maximal inhibition concentration IC(50). For the most effective acridine derivatives we examined their interaction with DNA and their effect on cell viability in order to investigate their eventual influence on cells. We thus identified planar acridine derivatives with intensive anti-amyloid activity (IC(50) and DC(50) values in micromolar range), low cytotoxicity and weak ability to interfere with the processes in the cell. Our findings indicate that both the planarity and the tautomerism of the 9-aminoacridine core together with the reactive nucleophilic thiosemicarbazide substitution play an important role in the anti-amyloid activities of studied derivatives. The present findings favor the application of the selected active planar acridines in the treatment of amyloid-related diseases.
  Biochimica et Biophysica Acta 01/2011; 1810(4):465-74. · 4.66 Impact Factor