4 and 37 degrees C. NO release was catalyzed by anionic liposomes (DPPG, DOPG, DMPS, POPS and DOPA) and by mixed phosphatidylglycerol/phosphatidylcholine (DPPG/DPPC and

DOPG/DPPC) covesicles, while cationic liposomes derived from 1,2-dioleoyl-3-trimethylammonium-propane (DOTAP) and the zwitterionic liposome DMPC did not significantly affect the dissociation rates of the substrates examined. Enhancement of the dissociation rate constant in DPPG liposome media (0.010 M phosphate buffer, pH 7.4, 37 degrees C) at 10 mM phosphoglycerol levels, ranged from 37 for 1 to 1.2 for the anionic diazeniumdiolate 4, while DOPA effected the greatest rate enhancement, GSK1904529A achieving 49-fold rate increases with 1 under similar conditions. The observed catalysis decreases with increase in the bulk concentration of electrolytes in the reaction media. Quantitative analysis of catalytic effects has been obtained through the application of pseudo-phase kinetic models and equilibrium binding constants at different liposome interfaces are compared. The stoichiometry of nitric oxide release from I and 2 Copanlisib in DPPG/DPPC liposome media has been obtained through oxyhemoglobin assay. DPPG = 1,2-dipalmitoyl-sn-glycero-3-[phospho-rac-(1-glycerol)], DOPG = 1,2-dioleoyl-sn-glycero-3-[phospho-rac-(1- -glycerol)], DM PS = 1,2-dimyristoyl-sn-glycero-3-[phospho-L-serine], POPS = 1-palmitoyl-2-oleoyl-sn-glycero-3[phospho-L-serine],

DOPA = 1,2-dioleoyl-sn-glycero-3-phosphate; DPPC = 1,2-dipalmitoyl-sn-glycero-3-phosphocholine, DMPC 1,2-dimyristoyl-sn-glycero-3-phospliocholine, DOTAP – 1,2-dioleoyl-3-trimetliylammonium-propane. (C)

2007 Elsevier Inc. All rights reserved.”
“Antibody fragments to the four Dengue virus serotypes were isolated from a human universal naive library using phage display technology. Phage-displayed antibody fragments were selected on Dengue virus particles directly captured from infected Vero cells supernatant by an anti-dengue monoclonal antibody, in order to avoid laborious virus concentration/purification procedures. A total of nine phage-displayed antibody fragments were obtained. Seven of them were highly specific for three of the selector serotypes (two for Dengue 1, four for Dengue 3 and one for Dengue 4). One clone (Dengue 3-selected) cross-reacted with Dengue 1, whereas another (selected with Dengue 2) cross-reacted with the three remaining serotypes. The soluble variants of six antibody PCI-34051 molecular weight fragments recognized their target viruses when used at nanomolar and even subnanomolar concentrations. All phage-displayed antibody fragments were cross-reactive against several strains of distinct genotypes within the corresponding serotype(s). These antibody fragments are potentially useful for the future development of tools for viral diagnosis and serotype identification. The simple phage selection method on captured virus could be applied in a high throughput way to obtain larger panels of antibody fragments to Dengue virus for multiple applications.