[en] The technology of obtaining pure and disperse molybdenum disulfide is worked out. The processes of refinement from the flotation reagents and deslimation by means of decantation, refinement of molybdenite concentrate from impurities by selective leaching methods are studied. The optimal regime of technological process is chosen

[en] A reproducible electro-assisted method is proposed to follow the influence of different sulfur-based anchoring groups on the adsorption kinetics and thermodynamics of SAM formation on gold electrodes. This has been made possible thanks to the preparation of several molecules containing various anchoring groups (thiol, thioester, acyclic and cyclic disulfides, thiosulfonate) while preserving the same spacer redox head group. In this paper we focus on the question of a substantial difference between SAMs derived from either alkylthiols or disulfides using cyclic voltammetry. The comparison of equilibrium surface coverage, affinity constant toward gold surface and stability suggest a decisive role of the nature of the anchoring group in the formation of the monolayers. Moreover, a significant difference of the desorption behavior of SAMs on gold, pre-formed from either thiol or disulfide, has clearly been demonstrated.

No abstract available

[en] To the best of our knowledge, however, the niobium analogue of this phase, NbPS₆ has not been discovered yet. As a result of efforts to find new phases in this family, we were able to prepare a new phase with disordered metals with the halide flux method. Here, we report the synthesis and structure of a new mixed-metal disulfide thiophosphate, Nb_0.44Ta_0.56PS₆. Crystallographic data for Nb_0.44Ta_0.56PS₆ are given in Table 1. Selected interatomic distances and angles are given in Tables 3. The title compound is isostructural with the previously reported TaPS₆ and its structure is closely related to those of the quaternary alkali metal thiophosphates such as K_0.38TaPS₆, A₂Nb₂P₂S₁₂ (A = K, Rb), K_0.18TaPS₆, K_0.28TaPS₆, and Rb_0.09TaPS₆. As shown in other group 5 transition metal thiophosphates, the structure of the title compound is made up of the bicapped trigonal biprismatic [M₂S₁₂] unit (M = Nb, Ta) and the tetrahedral [PS₄] group. This structural motif has already been encountered in other group 5 metal (V, Nb, Ta) thiophosphates such as RbNb₂PS₁₀. In the title structure, the metal(M) site is occupied by statistically disordered Nb (0.44(1)%) and Ta (0.56(1)%) atoms. The metal atom is surrounded by eight S atoms in a bicapped trigonal prismatic arrangement

[en] A convenient approach for synthesis of dendrimetric peptides is proposed. The strategy was developed by using unprotected dimeric peptides as building blocks. Our model involved the direct synthesis of a Cysteine containing dimer peptide and subsequent sulfhydryl group oxidation. The disulfide bridge formation reaction to get 90 amino acid residues tetrameric molecule is performed with dimethyl sulfoxide. This kind of dendrimetric peptide synthesis is called Double Dimer Construction System, and could be applied to obtain synthetic vaccines

[en] The crystal structure of the DsbB–DsbA–ubiquinone ternary complex has revealed a mechanism of protein disulfide bond generation in Escherichia coli. Protein disulfide bond formation is catalyzed by a series of Dsb enzymes present in the periplasm of Escherichia coli. The crystal structure of the DsbB–DsbA–ubiquinone ternary complex provided important insights into mechanisms of the de novo disulfide bond generation cooperated by DsbB and ubiquinone and of the disulfide bond shuttle from DsbB to DsbA. The structural basis for prevention of the crosstalk between the DsbA–DsbB oxidative and the DsbC–DsbD reductive pathways has also been proposed

[en] Data on protective groups for the thiol function of cysteine and methods of disulfide bonds formation used in modern peptide chemistry are considered and systematised. The advantages and disadvantages of protective groups, of reagents used for cyclisation, and possible side reactions associated with them are described. The bibliography includes 119 references.

[en] Highlights: • Protein Disulfide Isomers can interact with α11 integrin in response to adhesion. • Complexes PDI- α11 are linked by disulfide bonds. • Free thiol blockers and PDI inhibitors blocks adhesion and migration mediated by α11 integrin. Integrins belong to a family of transmembrane receptors that mediate cell migration and adhesion to ECM. Extracellular domains of integrin heterodimers contain cysteine-rich regions, which are potential sites of thiol-disulfide exchanges. Rearrangements of extracellular disulfide bonds regulate activation of integrin receptors by promoting transition from an inactive state into a ligand-binding competent state. Modifications of integrin disulfide bonds dependent on oxidation-reduction can be mediated by Protein Disulfide Isomerse (PDI). This paper provides evidences that binding to integrin ligands initiate changes in free thiol pattern on cell surface and that thiol-disulfide exchange mediated by PDI leads to activation of integrin subunit α11. By employing co-immunoprecipitation and confocal microscopy analysis we showed that α11β1 and PDI create complexes bounded by disulfide bonds. Using surface plasmon resonance we provide biochemical evidence that PDI can interact directly with integrin subunit α11.

[en] Highlights: ► MPH was genetically modified at its C-terminal with (Gly-Ser)₅–Cys. ► MPH-L was immobilized with fixed orientation via disulfide chemistry. ► The immobilized MPH-L retained the activity of MPH. ► MPH-L formed a homogeneous template. ► Homogeneous MIP film was obtained with orientated immobilization of the template. - Abstract: A method for preparing homogeneous protein-imprinted polymer films with orientated immobilization of template is described. The template methyl parathion hydrolase (MPH) was modified with a peptide linker (Gly-Ser)₅–Cys and was immobilized on a cover glass with a fixed orientation via the linker. The activity of the fusion enzyme (MPH-L) was evaluated by determining the product's absorbance at 405 nm (A₄₀₅). Both the free and the immobilized MPH-L showed higher retention of the bioactivity than the wide type enzyme (MPH-W) as revealed by the A₄₀₅ values for MPH-L_free/MPH-W_free (1.159/1.111) and for MPH-L_immobilized/MPH-W_immobilized (0.348/0.118). The immobilized MPH-L also formed a more homogeneous template stamp compared to the immobilized MPH-W. The molecularly imprinted polymer films prepared with the immobilized MPH-L exhibited high homogeneity with low Std. Deviations of 80 and 200 from the CL intensity mean volumes which were observed for batch-prepared films and an individual film, respectively. MPH-L-imprinted polymer film also had a larger template binding capacity indicated by higher CL intensity mean volume of 3900 INT over 2500 INT for MPH-W-imprinted films. The imprinted film prepared with the orientated immobilization of template showed an imprinting factor of 1.7, while the controls did not show an imprinting effect.

[en] In this study, we analyzed the properties of Cu films electrodeposited with 3-N,N-dimethylaminodithiocarbamoyl-1-propanesulfonate (DPS) as an organic additive in damascene Cu electrodeposition, in comparison with bis(sulfopropyl) disulfide (SPS). It was observed that the resistivity of Cu film electrodeposited with DPS was lower than that with SPS. Spectroscopic analyses showed that the impurity level and crystallinity of Cu films are almost the same, but the difference was found in the film roughness. Low roughness of Cu film electrodeposited with DPS led to the low resistivity, and it was speculated that the low roughness is related to the strong adsorption through the nitrogen atom in the DPS molecule.