Effect of Fe(3)O(4) magnetic nanoparticles on lysozyme amyloid aggregation.
Peptide amyloid aggregation is a hallmark of several human pathologies termed amyloid diseases. We have investigated the effect of electrostatically stabilized magnetic nanoparticles of Fe(3)O(4) on the amyloid aggregation of lysozyme, as a prototypical amyloidogenic protein. Thioflavin T fluorescence assay and atomic force microscopy were used for monitoring the inhibiting and disassembly activity of magnetic nanoparticles of Fe(3)O(4). We have found that magnetic Fe(3)O(4) nanoparticles are able to interact with lysozyme amyloids in vitro leading to a reduction of the amyloid aggregates, thus promoting depolymerization; the studied nanoparticles also inhibit lysozyme amyloid aggregation. The ability to inhibit lysozyme amyloid formation and promote lysozyme amyloid disassembly exhibit concentration-dependent characteristics with IC50 = 0.65 mg ml(-1) and DC50 = 0.16 mg ml(-1) indicating that nanoparticles interfere with lysozyme aggregation already at stoichiometric concentrations. These features make Fe(3)O(4) nanoparticles of potential interest as therapeutic agents against amyloid diseases and their non-risk exploitation in nanomedicine and nanodiagnostics.
Bellova
Andrea
A
Department of Biophysics, Department of Magnetism, Institute of Experimental Physics, Slovak Academy of Science, Kosice, Slovakia.
Bystrenova
Eva
E
Koneracka
Martina
M
Kopcansky
Peter
P
Valle
Francesco
F
Tomasovicova
Natalia
N
Timko
Milan
M
Bagelova
Jaroslava
J
Biscarini
Fabio
F
Gazova
Zuzana
Z
D000686:Amyloidosis / Q000188:drug therapy; D000818:Animals; D002645:Chickens; D052203:Ferrosoferric Oxide / Q000737:chemistry / Q000494:pharmacology*; D006801:Humans; D008280:Magnetics; D009113:Muramidase / Q000737:chemistry*; D053758:Nanoparticles / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D012995:Solubility
D009113:Muramidase; D052203:Ferrosoferric Oxide