RESUMO
Many synthetic or natural fibers are produced via the transformation of a liquid solution into a solid filament, which allows the wet processing of high molecular weight polymers, proteins, or inorganic particles. Synthetic wet-spun fibers are used in our everyday life from clothing to composite reinforcement applications. Spun fibers are also common in nature. Silk solidification results from the coagulation of protein solutions. The chemical phenomena involved in the formation of all these classes of fibers can be quite different but they all share the same fundamental transformation from a liquid to a solid state. The solidification process is critical because it governs the production rate and the strength that fibers can sustain to be drawn and wound. An approach is proposed in this work to investigate the kinetics of fiber solidification. This approach consists in circulating solidifying fibers in the extensional flow of a surrounding liquid. Such as polymers in extensional flows, the fibers break if resultant drag forces exceed the fiber tensile strength. The solidification kinetics of nanotube composite fibers serves as a validation example of this approach. The method could be extended to other systems and advance thereby the science and technology of fiber and textile materials. It is also a way to directly visualize the scission of chain-like systems in extensional flows.
RESUMO
As-produced carbon nanotubes often contain a fraction of impurities such as metal catalysts, inorganic supports, and carbon by-products. These impurities can be partially removed by using acidic dissolution. The resulting nanotube materials have to be dried to form a powder. The processability of nanotubes subjected to regular (thermal vaporisation) drying is particularly difficult because capillary forces pack and stick the nanotubes irreversibly, which limits their dispersability in polymeric matrices or solvents. We show that this dramatic limitation can be circumvented by using freeze-drying instead of regular-drying during nanotube purification process. In this case, the nanotubes are trapped in frozen water which is then sublimated. As a result the final powder is significantly less compact and, more important, the nanotubes can be easily dispersed with no apparent aggregates, thereby greatly enhancing their processability, e.g., they can be used to make homogeneous composites and fibers. Results from coagulation spinning from water-based dispersions of regularly-dried and freeze-dried nanotubes are compared. We also show that freeze-dried materials, in contrast to regularly-dried materials, can be dissolved in organic polar solvents using alkali-doped nanotubes. High resolution TEM and XRD analysis demonstrate that the nanotube structure and quality are not affected at the nanoscale by freeze-drying treatments.
Assuntos
Nanotecnologia/métodos , Nanotubos de Carbono/química , Química Farmacêutica/métodos , Liofilização , Congelamento , Microscopia Eletrônica de Transmissão , Nanotubos/química , Tamanho da Partícula , Solventes/química , Temperatura , Água/química , Difração de Raios XRESUMO
We report a new hot-drawing process for treating wet-spun composite fibers made of single- and multiwall carbon nanotubes and poly(vinyl alcohol). As shown in previous reports, untreated composite nanotube fibers exhibit a very large strain-to-failure, and their toughness, which is the energy needed to break the fibers, exceeds that of any other known materials. However, untreated composite nanotube fibers absorb a very small amount of energy at low strain and become degraded in humid conditions. In this work, we use hot-drawing treatments, a concept inspired from textile technologies, to improve the properties of nanotube/PVA fibers. This treatment yields a crystallinity increase of the PVA and an unprecedented degree of alignment of the nanotubes. These structural modifications lead to a markedly improved energy absorption at low strain and make the fibers resistant to moisture. Hot-drawn nanotube/PVA fibers hold great potential for a number of applications such as bulletproof vests, protective textiles, helmets, and so forth.
RESUMO
Percolation is a statistical concept that describes the formation of an infinite cluster of connected particles or pathways. Lowering the percolation threshold is a critical issue to achieve light and low-cost conductive composites made of an insulating matrix loaded with conductive particles. This has interest for applications where charge dissipation and electrical conductivity are sought in films, coatings, paints, or composite materials. One route to decreasing the loading required for percolation is to use rod-like particles. Theoretical predictions indicate that this may also be achieved by altering the interaction potential between the particles. Although percolation may not always respond monotonically to interactions, the use of adhesive rods can be expected to be an ideal combination. By using a system made of carbon nanotubes in an aqueous surfactant solution, we find that very small attraction can markedly lower the percolation threshold. The strength of this effect can thereby have direct technological interest and explain the large variability of experimental results in the literature dealing with the electrical behavior of composites loaded with conducting rods.
RESUMO
Protein structure determination by classical x-ray crystallography requires three-dimensional crystals that are difficult to obtain for most proteins and especially for membrane proteins. An alternative is to grow two-dimensional (2D) crystals by adsorbing proteins to ligand-lipid monolayers at the surface of water. This confined geometry requires only small amounts of material and offers numerous advantages: self-assembly and ordering over micrometer scales is easier to obtain in two dimensions; although fully hydrated, the crystals are sufficiently rigid to be investigated by various techniques, such as electron crystallography or micromechanical measurements. Here we report structural studies, using grazing incidence synchrotron x-ray diffraction, of three different 2D protein crystals at the air-water interface, namely streptavidine, annexin V, and the transcription factor HupR. Using a set-up of high angular resolution, we observe narrow Bragg reflections showing long-range crystalline order in two dimensions. In the case of streptavidin the angular range of the observed diffraction corresponds to a resolution of 10 A in plane and 14 A normal to the plane. We show that this approach is complementary to electron crystallography but without the need for transfer of the monolayer onto a grid. Moreover, as the 2D crystals are accessible from the buffer solution, the formation and structure of protein complexes can be investigated in situ.
Assuntos
Proteínas de Ligação a DNA , Proteínas/química , Água/química , Ar , Anexina A5/química , Anexina A5/efeitos da radiação , Proteínas de Bactérias/química , Proteínas de Bactérias/efeitos da radiação , Biotinilação , Toxina da Cólera/química , Toxina da Cólera/efeitos da radiação , Cristalografia por Raios X/métodos , Gangliosídeo G(M1)/química , Glutaral/química , Ligantes , Níquel/química , Fosfolipídeos , Proteínas/efeitos da radiação , Estreptavidina/química , Estreptavidina/efeitos da radiação , Síncrotrons , Fatores de Transcrição/química , Fatores de Transcrição/efeitos da radiação , Difração de Raios XRESUMO
Living cells contain a very large amount of membrane surface area, which potentially influences the direction, the kinetics, and the localization of biochemical reactions. This paper quantitatively evaluates the possibility that a lipid monolayer can adsorb actin from a nonpolymerizing solution, induce its polymerization, and form a 2D network of individual actin filaments, in conditions that forbid bulk polymerization. G- and F-actin solutions were studied beneath saturated Langmuir monolayers containing phosphatidylcholine (PC, neutral) and stearylamine (SA, a positively charged surfactant) at PC:SA = 3:1 molar ratio. Ellipsometry, tensiometry, shear elastic measurements, electron microscopy, and dark-field light microscopy were used to characterize the adsorption kinetics and the interfacial polymerization of actin. In all cases studied, actin follows a monoexponential reaction-limited adsorption with similar time constants (approximately 10(3) s). At a longer time scale the shear elasticity of the monomeric actin adsorbate increases only in the presence of lipids, to a 2D shear elastic modulus of mu approximately 30 mN/m, indicating the formation of a structure coupled to the monolayer. Electron microscopy shows the formation of a 2D network of actin filaments at the PC:SA surface, and several arguments strongly suggest that this network is indeed causing the observed elasticity. Adsorption of F-actin to PC:SA leads more quickly to a slightly more rigid interface with a modulus of mu approximately 50 mN/m.
Assuntos
Actinas/química , Actinas/metabolismo , Actinas/ultraestrutura , Adsorção , Animais , Fenômenos Biofísicos , Biofísica , Biopolímeros/química , Biopolímeros/metabolismo , Galinhas , Elasticidade , Técnicas In Vitro , Cinética , Lipídeos de Membrana/química , Lipídeos de Membrana/metabolismo , Microscopia Eletrônica , Propriedades de Superfície , Tensão SuperficialRESUMO
We present here some sensitive optical and mechanical experiments for monitoring the process of formation and growth of two-dimensional (2D) crystals of proteins on a lipid monolayer at an air-water interface. The adsorption of proteins on the lipid monolayer was monitored by ellipsometry measurements. An instrument was developed to measure the shear elastic constant (in plane rigidity) of the monolayer. These experiments have been done using cholera toxin B subunit (CTB) and annexin V as model proteins interacting with a monosialoganglioside (GM1) and dioleoylphosphatidylserine (DOPS), respectively. Electron microscopy observations of the protein-lipid layer transferred to grids were systematically used as a control. We found a good correlation between the measured in-plane rigidity of the monolayer and the presence of large crystalline domains observed by electron microscopy grids. Our interpretation of these data is that the crystallization process of proteins on a lipid monolayer passes through at least three successive stages: 1) molecular recognition between protein and lipid-ligand, i.e., adsorption of the protein on the lipid layer; 2) nucleation and growth of crystalline patches whose percolation is detected by the appearance of a non-zero in-plane rigidity; and 3) annealing of the layer producing a slower increase of the lateral or in-plane rigidity.