In this work the 4-(trans-$4^{\prime }\text{−}n$-hexylcyclohexyl)-isothiocyanatobenzene (6CHBT) liquid crystal was doped with differently shaped magnetite nanoparticles. The structural changes were observed by capacitance measurements and showed significant influence of the shape and size of the magnetic particles on the magnetic Fréedericksz transition. For the volume concentration $\varphi =2\times {10}^{-4}$ of the magnetic particles, the critical magnetic field was established for the pure liquid crystal, and for liquid crystals doped with spherical, chainlike, and rodlike magnetic particles. The influence of the magnetic field depends on the type of anchoring, which is characterized by the density of anchoring energy and by the initial orientation between the liquid crystal molecules and the magnetic moment of the magnetic particles. The experimental results indicated soft anchoring in the case of spherical magnetic particles and rigid anchoring in the case of rodlike and chainlike magnetic particles, with parallel initial orientation between the magnetic moments of the magnetic particles and director.

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.