Hydrogen diffusion on (100), (111), (110) and (211) gold faces

Calculations showed that hydrogen adsorption into subsurface sites is most likely to occur on Au (110) and (211) faces. The presence of low-coordinated Au atoms on significantly reduces the barrier of subsurface adsorption of H. The barriers of H surface diffusion increase in the following Au series: (110) < (111) < (100) < (211). An analysis of the dependence of the surface diffusion barriers on the electronic structure of gold atoms on the respective faces revealed a U-shaped dependence of the centers of the s- and d-bands. This dependence is the result of the filling of the s- and d-bands on different faces of the gold. The results obtained suggest that it is possible to use band centers to determine surface diffusion barriers.     

Hypokinetic stress and neuronal porosome complex in the rat brain: the electron microscopic study

Porosomes are the universal secretory machinery in cells, where membrane-bound secretory vesicles transiently dock and fuse to release intravesicular contents to the outside of the cell during cell secretion. Studies using atomic force microscopy, electron microscopy, electron density and 3D contour mapping, provided rich nanoscale information on the structure and assembly of proteins within the neuronal porosome complex in normal brain. However it remains uncertain whether pathological conditions that alter process of neurotransmission, provoke alterations in the porosome structure also. To determine if porosomes are altered in disease states, the current study was undertaken for first time using high resolution electron microscope. One of pathologies that produce subtle alteration at the presynaptic terminals has been demonstrated to be hypokinetic stress. The central nucleus of amygdale is the brain region, where such alterations are mostly expressed. We have examined the width and depth of the neuronal porosome complex and their alterations provoked by chronic hypokinetic stress in above mentioned limbic region. Specifically, we have demonstrated that despite alterations in the presynaptic terminals and synaptic transmission provoked by this pathological condition in this region, the final step/structure in neurosecretion--the porosome--remains unaffected: the morphometric analysis of the depth and diameter of this cup-shaped structure at the presynaptic membrane point out to the heterogeneity of porosome dimensions, but with unchanged fluctuation in norm and pathology.     

From 1,4-diketones to N-vinyl derivatives of 3,3′-bipyrroles and 4,8-dihydropyrrolo[2,3-f]indole in just two preparative steps

Dioximes of hexane-2,5-dione and cyclohexane-1,4-dione react with acetylene in an autoclave (KOH/DMSO, 100 °C, 1 h, initial pressure 14 atm) to give 2,2′-dimethyl-1,1′-divinyl-[3,3′]bipyrrole and 1,5-divinyl-4,8-dihydropyrrolo[2,3-f]indole in 12% and 6% yields, respectively, thus exemplifying a very simple, straightforward route to inaccessible or unknown pyrrolic assemblies.     

6alpha-Angeloylplatynecine: a new alkaloid from Senecio nemorensis subsp. fuchsii (C.C. Gmelin) celak

The new alkaloid 6alpha-angeloylplatynecine, together with other four known pyrrolizidine alkaloids was identified from above ground parts of Senecio nemorensis subs. fuchsii.     

Regulating aspects of biosoluble and insoluble film release systems containing protein proteinase inhibitor

New types of potent aprotinin-containing medicinal polymer films are elaborated for topical applications. The higher the temperature of drying, the lower the steam absorption, the film swelling, and the velocity of aprotinin in vitro release. The presence of antimicrobials having the basic functional groups contributed to compacting the structure of the films and retention of aprotinin in them. The velocity of aprotinin release from the films is regulated by adding different polymers. Inclusion of polyvinylpirrolidone in the film resulted in acceleration and increase of aprotinin release. This was probably because of increasing the film swelling by a factor of 1.7. Additional retention of the inhibitor in films was achieved by inclusion of sodium alginate and cellulose powder capable of binding aprotinin. Soluble bioadhesive films derived from a copolymer of acrylamide,N-vinyl-pirrolidone, ethyl acrylate (M _r 30,000-600,000) and aprotinin were obtained and analyzed. Kinetics of aprotinin release from biosoluble films was studied under various conditions. The duration of aprotinin release was comparable with duration of gradual dissolution of the matrix. Bioavailability of aprotinin from soluble films was linear with time.