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A V Goncharenko

Publications and source records attributed to A V Goncharenko.

8 recordsLinked to original sources
PubMed2006

Electric near-field enhancing properties of a finite-size metal conical nano-tip.

Finite-difference time-domain (FDTD) technique simulations are performed to study the near-field resonance properties of a silver conical nano-tip with a rounded end. Varying the tip geometry, we have computed the electric field distribution, as well as the electric field enhancement factor in the immediate vicinity of the tip apex. The aim of this study is to find optimal geometric parameters of the conical tip, such as its angle and length, in order to maximize the electric field enhancement factor. The increase of the tip length is shown to result in a redshift of the tip resonance wavelength. In addition, some subsidiary (non-dipole) peaks appear for relatively long tips. The peak enhancement values for the small-angle tips increase with the tip length while those for the large-angle ones decrease with it. At the same time, the dependencies of the field enhancement on the cone angle exhibit non-monotonic behavior. In other words, an optimal angle exists allowing one to maximize the electric near field. Finally, the effect of the supporting dielectric medium on the electric field near the tip apex is discussed. In the approximation used, the effect is shown to leave the main conclusions unchanged.

Journal Article↗
PubMed2006

Proteins of the Rpf (resuscitation promoting factor) family are peptidoglycan hydrolases.

The secreted Micrococcus luteus protein, Rpf, is required for successful resuscitation of dormant "non-culturable" M. luteus cells and for growth stimulation in poor media. The biochemical mechanism of Rpf action remained unknown. Theoretical predictions of Rpf domain architecture and organization, together with a recent NMR analysis of the protein structure, indicate that the conserved Rpf domain has a lysozyme-like fold. In the present study, we found that both the secreted native protein and the recombinant protein lyse crude preparations of M. luteus cell walls. They also hydrolyze 4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside, a synthetic substrate for peptidoglycan muramidases, with optimum activity at pH 6. The Rpf protein also has weak proteolytic activity against N-CBZ-Gly-Gly-Arg-beta-naphthylamide, a substrate for trypsin-like enzymes. Rpf activity towards 4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside was reduced when the glutamate residue at position 54, invariant for all Rpf family proteins and presumably involved in catalysis, was altered. The same amino acid substitution resulted in impaired resuscitation activity of Rpf. The data indicate that Rpf is a peptidoglycan-hydrolyzing enzyme, and strongly suggest that this specific activity is responsible for its growth promotion and resuscitation activity. A possible mechanism of Rpf-mediated resuscitation is discussed.

Bacterial Proteins↗
PubMed2005

Preparation and optical properties of Au/Teflon nanocomposites.

Using thermal deposition technique, we have prepared Au/Teflon thin films on glass substrates. To control the film microstructure, both TEM and AFM characterization have been carried out. The visible optical transmission spectra have been measured in-situ. The peak positions and linewidths in the spectra have been identified in terms of the gold nanoparticle shape, size, and arrangement. The results obtained provide evidence for formation of both sphere-like and cylinder-like gold nanoparticles in the films. The fraction of each kind of the particles depends on whether the plasma treatment has been used. The treatment is shown to enhance the fraction of the cylinder-like particles.

Biocompatible Materials↗
PubMed2004

Percolation threshold for Bruggeman composites.

Using a simple phenomenological approach, we calculate the percolation threshold for Bruggeman composites having microgeometry of two kinds. Both kinds of composites consist of spheroids whose shape follows the Beta distribution. At the same time, the first one is a mixture of spheroids equally oriented along their revolution axis. In this case the percolation threshold is shown to be the same as for an assembly of equally oriented identical spheroids whose shape corresponds to the most probable shape of the distribution. For such composites the percolation threshold can vary between 0 and 1. The second one is a random mixture of the spheroids. In this case the percolation threshold is expressed in terms of the Gauss hypergeometric function; it is shown to vary between 0 and 1/3. The derived analytical results are supplemented with numerical calculations carried out for different values of the Beta distribution parameters.

Journal Article↗
PubMedDate not supplied

[Common epitopes of protein antigens in Neisseria and Moraxella].

Cross reactions between N. meningitidis and M. catarrhalis proteins were studied with the use of a panel of monoclonal antibodies to M. catarrhalis protein antigens. All antigenic preparations under study were shown to give cross reactions between N. meningitidis serotype porin of 39 kD (strain B125) and M. catarrhalis proteins of 40-41 kD. These M. catarrhalis proteins belonged to main proteins of class F and had the function of porins in the cell. In addition, the epitope of 41-kD antigen, detected by monoclonal antibodies 3E10, is common for both N. meningitidis porin and N. meningitidis iron-regulated proteins of 70 and 50 kD. The epitope of M. catarrhalis protein of 67 kD, detected by monoclonal antibodies 1G6, is common for N. meningitidis porin and N. meningitidis iron-regulated proteins of 50 and 55 kD.

Antibodies, Monoclonal↗
PubMedDate not supplied

[Properties of 2-C-methyl-D-erythritol 2,4-cyclopyrophosphate--an intermediate in the non-mevalonate isoprenoid biosynthesis].

Extraction and purification from the biomass of Corynebacterium ammoniagenes of 2-C-methyl-D-erhythritol 2,4-cyclopyrophosphate (MEC) was associated with its spontaneous transformation into a number of derivatives (which was due to pyrophosphate bond lability and the formation of complexes with metals). These derivatives included 1,2-cyclophospho-4-phosphate, 2,4-diphosphate, 2,3-cyclophosphate, 1,4-diphosphate, and 3,5-diphosphate (identified by 1H, 31P, and 13C NMR spectroscopy) and accounted for about 10% MEC. When added to a solution of DNA in the presence of the Fenton reagent, MEC prevented DNA decomposition. In addition, MEC slowed down the interaction of the reagent with tempol radicals, which indicates that complexation of ferrous ions by MEC attenuates their ability to catalyze the formation of hydroxyl radicals from hydrogen peroxide. In the presence of 0.23 mM MEC, the rate of respiration of rat liver mitochondria increased 1.8 times. At 0.1-1.0 mM, MEC activated in vitro proliferation of human Vgamma9 T-cells. It is suggested that MEC acts as an endogenous stabilizing agent for bacterial cells subjected to oxidative stress and as an immunomodulator for eukaryotic hosts.

Adjuvants, Immunologic↗