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Diameter Fibers (diameter + fiber)

Distribution by Scientific Domains

Polymers and Materials Science	50%
Medical Sciences	50%

Selected Abstracts

Production of Submicrometer Diameter Fibers by Two-Fluid Electrospinning,

ADVANCED MATERIALS, Issue 17 2004
H. Yu
Electrospinning of nanofibers of materials that are difficult to process using conventional techniques is reported. Two fluids are electrospun (see Figure) into fibers with core/shell morphology. The "electrospinnable" shell fluid serves as a process aid to electrospin the core fluid. Three examples are illustrated: production of fibers with diameters less than 100 nm, fibers formed of low-molecular-weight polyaniline, and non-blended electrospun silk fibers. [source]

Organic and aqueous compatible polystyrene,maleic anhydride copolymer ultra-fine fibrous membranes

JOURNAL OF APPLIED POLYMER SCIENCE, Issue 2 2009
Corine Cécile
Abstract Polystyrene,maleic anhydride copolymer (PSMA, Mv= 700 kDa) was synthesized and efficiently processed into 400 to 600 nm diameter fibers via electrospinning from either 20 wt % dimethylformamide or 25 wt % dimethylsulfoxide solution. Crosslinking of PSMA was effective by adding glycerol and poly(vinyl alcohol) (PVA) (Mw = 31,50 kDa) in the dimethylformamide and dimethylsulfoxide solutions, respectively. The PSMA fibers containing glycerol at 29.4 mol% were auto-crosslinked whereas those with 12.9 mol% (2 wt %) glycerol and 15.4 mol% (0.75 wt %) PVA required heating to induce intermolecular esterification. Heat-induced crosslinking with glycerol was more effective in rendering the PSMA fibrous membranes insoluble in all solvents whereas that with PVA remained soluble in most solvents except for acetone and tetrahydrofuran. The crosslinked fibrous membranes had improved thermally stability and retained physical integrity upon exposure (2 hr at 40°C) to carbon disulfide, the solvent for Friedel-Craft reactions of the styrene moiety. Hydrolysis (0.01N NaOH) of the auto-crosslinked fibrous membrane significantly improved its hydrophilicity by reducing the water contact angles from 90.6° to 62.5° in a matter of seconds. These ultra-high specific surface PSMA fibrous membranes have shown superior organic and aqueous solvent compatibility to be used as highly reactive and easily retrievable supports for solid-phase synthesis. © 2009 Wiley Periodicals, Inc. J Appl Polym Sci, 2009 [source]

Myelin thickenings in val 102/fs null mutation of MPZ gene

JOURNAL OF THE PERIPHERAL NERVOUS SYSTEM, Issue 2 2004
MV De Angelis
Myelin thickenings, abnormal myelin foldings and tomacula have been rarely described in CMT1B. In two unrelated patients of different age (patient 1: 29 years old; patient 2: 65 years old) with CMT1B and Val 102/fs null mutation of MPZ gene we performed morphometric analysis, teased fibers and ultrastructural examination of sural nerve. We found: 1) markedly decreased fiber density with prevalent loss of large diameter fibers (patient 1: 4419 fibers/mm2; patient 2: 1326 fibers/mm2); 2) evidence of de-remyelination; and 3) paranodal and internodal myelin thickenings in virtually all fibers. Patient 1 has myelin thickenings measuring more than 50% of the fiber diameter in 14% of fibers and thickenings greater than 30% in 33% of fibers. Patients 2 presents myelin thickenings measuring more than 50% of fiber diameter in 23% of fibers and thickening greater than 30% in 49% of fibers. When considering the absolute measure of myelin thickenings and their number over 100 internodes, patient 1 presents 150 small myelin thickenings (<8 mm of diameter) whereas patient 2 has 57. The number of globules (8,12 mm of diameter) is 56 in patient 1 and 45 in patient 2. The number of myelin thickenings greater than 12 mm is 33 in patient 1 and 45 in patient 2. Ultrathin sections showed myelin infoldings, outfoldings and uncompacted myelin. CMT1B with a heterozygous null mutation of MPZ gene is characterized by abundant focal myelin thickenings. Similar findings have been described in the P0 deficient heterozygous mice. [source]

Incorporation of fibrin molecules containing fibrinopeptide A alters clot ultrastructure and decreases permeability

BRITISH JOURNAL OF HAEMATOLOGY, Issue 1 2007
Veronica H. Flood
Summary Previous studies have shown that a heterozygous mutation in the fibrinogen A, chain gene, which results in an A, R16C substitution, causes fibrinolytic resistance in the fibrin clot. This mutation prevents thrombin cleavage of fibrinopeptide A from mutant A, R16C chains, but not from wild-type A, chains. However, the mechanism underlying the fibrinolytic resistance is unclear. Therefore, this study investigated the biophysical properties of the mutant fibrin that contribute to fibrinolytic resistance. Fibrin clots made from the mutant fibrinogen incorporated molecules containing fibrinopeptide A into the polymerised clot, which resulted in a ,spiky' clot ultrastructure with barbed fibrin strands. The clots were less stiff than normal fibrin and were cross-linked slower by activated FXIII, but had an increased average fiber diameter, were more dense, had smaller pores and were less permeable. Protein sequencing showed that unclottable fibrinogen remaining in the supernatant consisted entirely of homodimeric A, R16C fibrinogen, whereas both cleaved wild-type , chains and uncleaved A, R16C chains were in the fibrin clot. Therefore, fibrinolytic resistance of the mutant clots is probably a result of altered clot ultrastructure caused by the incorporation of fibrin molecules containing fibrinopeptide A, resulting in larger diameter fibers and decreased permeability to fibrinolytic enzymes. [source]