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1.
J Am Chem Soc ; 130(33): 10880-1, 2008 Aug 20.
Article in English | MEDLINE | ID: mdl-18656916

ABSTRACT

In this communication, we report a novel preparation of the helical carbon nanofibril-fabricated thin film from the iodine-doped filmy helical polyacetylene through a carbonization process. Carbonization of the helical polyacetylene films by way of iodine doping is found to afford carbon and graphitic films completely preserving morphologies and even helical nanofibril structures.


Subject(s)
Graphite/chemical synthesis , Iodine/chemistry , Membranes, Artificial , Nanotubes, Carbon/chemistry , Polyynes/chemistry , Gas Chromatography-Mass Spectrometry , Graphite/chemistry , Models, Molecular , Nanotubes, Carbon/ultrastructure , Particle Size , Surface Properties , Temperature , Thermogravimetry , X-Ray Diffraction
2.
J Nanosci Nanotechnol ; 6(12): 3923-8, 2006 Dec.
Article in English | MEDLINE | ID: mdl-17256354

ABSTRACT

The fabrication of miscible or nanostructured polymer blends or alloys raises much hope, but poses significant scientific and industrial challenges over the past several decades. Here, we propose a novel strategy using high-shear processing and demonstrate the high-shear effects on the nanodispersed structure formed in the poly(vinylidene fluoride) (PVDF)/polyamide 11 (PAll) blends, in which PA11 domains with a size of several tens of nanometers are dispersed in the PVDF phase. For the blend of PVDF/PA11 = 65/35, the TEM image shows that many nanometer-sized PAl1 particles are dispersed in the PVDF domain to form a special type of domain-in-domain morphology. In contrast, no PVDF nano-dispersion was observed in the PA11 phase. The effects of both the screw rotation speed and the mixing time on the blend structure were systematically studied. It shows that the extruder screw rotation speed and the mixing time are two critical factors to prepare the nanostructured blends. In addition, the investigations on the thermal behavior of the obtained blends indicate the improved miscibility between PVDF and PAl1 by the high shear processing.


Subject(s)
Crystallization/methods , Nanostructures/chemistry , Nanostructures/ultrastructure , Nanotechnology/methods , Nylons/chemistry , Polyvinyls/chemistry , Colloids/chemistry , Macromolecular Substances/chemistry , Materials Testing , Molecular Conformation , Particle Size , Shear Strength , Stress, Mechanical , Surface Properties
3.
J Mol Biol ; 348(4): 983-98, 2005 May 13.
Article in English | MEDLINE | ID: mdl-15843028

ABSTRACT

Various mutants of the protein fragment, barnase module-1 (1-24) were investigated in order to reveal the structural principle of amyloid-like fibrils. By means of circular dichroism spectroscopy, X-ray diffraction, electron microscopy, and thioflavin T binding assay, we found that the molecules containing two beta-strands and an intervening turn structure are assembled to form a cross-beta structure. Stabilization by both the hydrophobic interactions and hydrogen bonding between the respective paired side-chains on the coupled beta-strands was essential for fibril formation. These two types of interaction can also arrange the corresponding residues in lines on both sheet surfaces of protofilaments with a cross-beta structure. This leads to the most probable fibril structure constructed with the line-matching interactions between protofilaments. Consideration of the geometrical symmetry resulted in our finding that a limited number of essential models for molecular packing in fibril structure are stable, which would rationally explain the occurrence of two or three morphologies from an identical molecular species. The ribbon-like fibrils exhibited striped texture along the axis, which was assigned to a stacked two-sheet repeat as a structural unit. The comprehensively proposed structural model, that is, the sheet-sheet interaction between left-handed cross-beta structures, results in a slightly right-handed twist of beta-sheet stacking, which reasonably elucidates the intrinsic sizes of the fibril width and its helical period along the fibril axis, as the bias in the orientation of the hydrogen-bonded beta-strand pair at the lateral edge is larger than that at the central protofilament.


Subject(s)
Amyloid/chemistry , Amyloid/metabolism , Amyloid/genetics , Amyloid/ultrastructure , Benzothiazoles , Circular Dichroism , Hydrogen Bonding , Hydrogen-Ion Concentration , Hydrophobic and Hydrophilic Interactions , Microscopy, Electron, Transmission , Models, Molecular , Mutation/genetics , Protein Structure, Quaternary , Stereoisomerism , Thiazoles/pharmacology , X-Ray Diffraction
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