ABSTRACT
A quantitative analysis of blurring and its dependence on the stencil-substrate gap and the deposition parameters in stencil lithography, a high resolution shadow mask technique, is presented. The blurring is manifested in two ways: first, the structure directly deposited on the substrate is larger than the stencil aperture due to geometrical factors, and second, a halo of material is formed surrounding the deposited structure, presumably due to surface diffusion. The blurring is studied as a function of the gap using dedicated stencils that allow a controlled variation of the gap. Our results show a linear relationship between the gap and the blurring of the directly deposited structure. In our configuration, with a material source of approximately 5 mm and a source-substrate distance of 1 m, we find that a gap size of approximately 10 microm enlarges the directly deposited structures by approximately 50 nm. The measured halo varies from 0.2 to 3 microm in width depending on the gap, the stencil aperture size and other deposition parameters. We also show that the blurring can be reduced by decreasing the nominal deposition thickness, the deposition rate and the substrate temperature.
Subject(s)
Nanostructures/chemistry , Nanotechnology/methods , Nanowires/chemistry , Microscopy, Electron, Scanning , Nanostructures/ultrastructure , Nanowires/ultrastructureABSTRACT
Aluminum and gold nanowires were fabricated using 100 mm stencil wafers containing nanoslits fabricated with a focused ion beam. The stencils were aligned and the nanowires deposited on a substrate with predefined electrical pads. The morphology and resistivity of the wires were studied. Nanowires down to 70 nm wide and 5 mum long have been achieved showing a resistivity of 10 microOmegacm for Al and 5 microOmegacm for Au and maximum current density of approximately 10(8) A/cm(2). This proves the capability of stencil lithography for the fabrication of metallic nanowires on a full wafer scale.
Subject(s)
Aluminum/chemistry , Gold/chemistry , Nanowires/chemistry , Nanowires/ultrastructure , Microscopy, Atomic Force , Silicon/chemistryABSTRACT
A modestly active, nonselective triarylimidazole lead was optimized for binding affinity with the human glucagon receptor. This led to the identification of a 2- and/or 4-alkyl or alkyloxy substituent on the imidazole C4-aryl group as a structural determinant for significant enhancement in binding with the glucagon receptor (e.g., 41, IC(50)=0.053 microM) and selectivity (>1000x) over p38MAP kinase in this class of compounds.
Subject(s)
Pyridines/chemistry , Pyridines/pharmacology , Receptors, Glucagon/antagonists & inhibitors , Animals , CHO Cells , Cricetinae , Drug Design , Drug Evaluation, Preclinical , Humans , Imidazoles/chemistry , Inhibitory Concentration 50 , Magnesium/metabolism , Magnesium/pharmacology , Mitogen-Activated Protein Kinases/drug effects , Mitogen-Activated Protein Kinases/metabolism , Pyridines/metabolism , Receptors, Glucagon/metabolism , Structure-Activity Relationship , p38 Mitogen-Activated Protein KinasesABSTRACT
Investigation of furans, pyrroles and pyrazolones identified 3-pyridyl-2,5-diaryl-pyrroles as potent, orally bioavailable inhibitors of p38 kinase. 3-(4-pyridyl-2-(4-fluoro-phenyl)-5-(4-methylsulfinylphenyl)-pyrrol e (L-167307) reduces secondary paw swelling in the rat adjuvant arthritis model: ID50 = 7.4 mg/kg/b.i.d.
