Thin Film ZnO as Sublayer for Electric Contact for Bulk GaN with Low Electron Concentration

Fabrication of low resistivity ohmic contacts to N polarity gallium nitride crystal is an important issue for the construction of the vertical current flow devices like laser diodes and high brightness light emitting diodes. Gallium nitride is a challenging material because of the high metal work function required to form a barrier-free metal-semiconductor interface. In practice, all useful ohmic contacts to GaN are based on the tunneling effect. Efficient tunneling requires high doping of the material. The most challenging task is to fabricate high quality metal ohmic contacts on the substrate because the doping control is here much more difficult that in the case of epitaxial layers. In the present work we propose a method for fabricating low resistivity ohmic contacts on N-side of GaN wafers grown by hydride vapor phase epitaxy. These crystals were characterized by a n-type conductivity and the electron concentration of the order of 10$\text{}^{17}$ cm$\text{}^{-3}$. The standard Ti/Au contact turned out to be unsatisfactory with respect to its linearity and resistance. Instead we decided to deposit high-n type ZnO layers (thickness 50 nm and 100 nm) prepared by atomic layer deposition at temperature of 200°C. The layers were highly n-type conductive with the electron concentration in the order of 10$\text{}^{20}$ cm$\text{}^{-3}$. Afterwards, the metal contact to ZnO was formed by depositing Ti and Au. The electrical characterization of such a contact showed very good linearity and as low resistance as 1.6 × 10$\text{}^{-3}$ Ω cm$\text{}^{2}$. The results indicate advantageous properties of contacts formed by the combination of the atomic layer deposition and hydride vapor phase epitaxy technology

The antigen-binding site of an N-propionylated polysialic acid-specific antibody protective against group B meningococci is consistent with extended epitopes

Monoclonal antibodies 13D9 and 6B9 are both specific for N-propionylated polysialic acid (NPrPSA); however, while 13D9 is protective against meningitis caused by group B meningococci and Escherichia coli capsular type K1 infection, 6B9 is not. The crystal structures of the Fabs from the two antibodies determined at 2.06 and 2.45 \uc5 resolutions, respectively, reveal markedly different combining sites, where only the surface of 13D9 is consistent with the recognition of extended helical epitopes known to exist in the capsular polysaccharides of etiological agents of meningitis. Interestingly, complementarity determining region H2 on 13D9 lies in a non-canonical conformation that docking studies show is a critical feature in the generation of negative free energy of binding. Finally, the model of extended NPrPSA decasaccharide bound to 13D9 derived from docking studies is consistent with saturation transfer difference nuclear magnetic resonance experiments. Together, these results provide further evidence that extended epitopes have the ability to break immune tolerance associated with the polysialic acid capsule of these pathogens.Peer reviewed: YesNRC publication: Ye

Studies of a murine monoclonal antibody directed against DARC: reappraisal of its specificity.

Duffy Antigen Receptor for Chemokines (DARC) plays multiple roles in human health as a blood group antigen, a receptor for chemokines and the only known receptor for Plasmodium vivax merozoites. It is the target of the murine anti-Fy6 monoclonal antibody 2C3 which binds to the first extracellular domain (ECD1), but exact nature of the recognized epitope was a subject of contradictory reports. Here, using a set of complex experiments which include expression of DARC with amino acid substitutions within the Fy6 epitope in E. coli and K562 cells, ELISA, surface plasmon resonance (SPR) and flow cytometry, we have resolved discrepancies between previously published reports and show that the basic epitope recognized by 2C3 antibody is 22FEDVW26, with 22F and 26W being the most important residues. In addition, we demonstrated that 30Y plays an auxiliary role in binding, particularly when the residue is sulfated. The STD-NMR studies performed using 2C3-derived Fab and synthetic peptide corroborated most of these results, and together with the molecular modelling suggested that 25V is not involved in direct interactions with the antibody, but determines folding of the epitope backbone

Rational chemical design of the carbohydrate in a glycoconjugate vaccine enhances IgM-to-IgG switching

Many pathogens are sheltered from host immunity by surface polysaccharides that would be ideal as vaccines except that they are too similar to host antigens to be immunogenic. The production of functional IgG is a desirable response to vaccines; because IgG is the only isotype that crosses the placenta, it is of particular importance in maternal vaccines against neonatal disease due to group B Streptococcus (GBS). Clinical studies found a substantially lower proportion of IgG—relative to IgM—among antibodies elicited by conjugates prepared with purified GBS type V capsular polysaccharide (CPS) than among those evoked by CPSs of other GBS serotypes. The epitope specificity of IgG elicited in humans by a conjugate prepared with type V CPS is for chemically desialylated type V CPS (dV CPS). We studied desialylation as a mechanism for enhancing the ability of type V CPS to induce IgM-to-IgG switching. Desialylation did not affect the structural conformation of type V CPS. Rhesus macaques, whose isotype responses to GBS conjugates match those of humans, produced functionally active IgG in response to a dV CPS–tetanus toxoid conjugate (dV-TT), and 98% of neonatal mice born to dams vaccinated with dV-TT survived lethal challenge with viable GBS. Targeted chemical engineering of a carbohydrate to create a molecule less like host self may be a rational approach for improving other glycoconjugates