Publications by authors named "A G Leonov"

I revisit the well-known phase transition between the hexagonal skyrmion lattice and the homogeneous state within the phenomenological Dzyaloshinskii theory for chiral magnets, which includes only the exchange, Dzyaloshinskii-Moriya, and Zeeman energy contributions. I show that, in a narrow field range near the saturation field, the hexagonal skyrmion order gradually transforms into a square arrangement of skyrmions. Then, by the second-order phase transition during which the lattice period diverges, the square skyrmion lattice releases a set of repulsive isolated skyrmions.

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The currently circulating S31N variant of the M2 proton channel of influenza A is resistant to antiviral drugs. Recently, there has been a growing concern regarding the impact of the lipid environment on the structural features of the S31N variant. The native symmetry of the M2 tetramer remains controversial.

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Article Synopsis
  • * The hexagonal skyrmion configuration transforms into a rhombic structure before arriving at a square arrangement, facilitated by the dynamics of merons and anti-merons at the skyrmion boundaries.
  • * I also investigate the role of domain-wall merons in the dynamics of square skyrmion lattices, examining spin-wave modes and their response to AC magnetic fields, revealing distinct rotation and annihilation patterns in merons at different frequencies.
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Mesoporous hydroxyapatite (HA) is widely used in various applications, such as the biomedical field, as a catalytic, as a sensor, and many others. The aim of this work was to obtain HA powders by means of chemical precipitation in a medium containing a polymer-polyvinyl alcohol or polyvinylpyrrolidone (PVP)-with concentrations ranging from 0 to 10%. The HA powders were characterized by X-ray diffraction, Fourier transform infrared spectroscopy, atomic emission spectroscopy with inductively coupled plasma, electron paramagnetic resonance, scanning electron microscopy (SEM), and transmission electron microscopy (TEM).

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Melanoma is the most serious and deadly form of skin cancer and with progression to advanced melanoma, the intrinsically disordered protein α-synuclein is upregulated to high levels. While toxic to dopaminergic neurons in Parkinson's disease, α-synuclein is highly beneficial for primary and metastatic melanoma cells. To gain detailed insights into this exact opposite role of α-synuclein in advanced melanoma, we performed proteomic studies of high-level α-synuclein-expressing human melanoma cell lines that were treated with the diphenyl-pyrazole small-molecule compound anle138b, which binds to and interferes with the oligomeric structure of α-synuclein.

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