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Deals with a study which examined the elastic properties of a unidirectional silicon carbide fiber. Significance of metal-matrix composites; Methodology; Micromechanics modeling; Results and discussion; Conclusions.

Unlike previous in vitro measurements where Amyloid β (Aβ) aggregation was studied in bulk solutions, we detect the structure change of the Aβ aggregate on the surface of a wireless quartz-crystal-microbalance biosensor, which resembles more closely the aggregation process on the cell membrane. Using a 58 MHz quartz crystal, we monitored changes in the viscoelastic properties of the aggregate formed on the quartz surface from monomers to oligomers and then to fibrils, involving up to the 7th overtone mode (406 MHz). With atomic-force microscopy observations, we found a significant stiffness increase as well as thinning of the protein layer during the structure change from oligomer to fibrils at 20 h, which indicates that the stiffness of the fibril is much higher. Viscoelasticity can provide a significant index of fibrillation and can be useful for evaluating inhibitory medicines in drug development. [ABSTRACT FROM AUTHOR]

Surface waves are often excited by interdigitated transducers consisting of many nanostrips attached on a substrate, and it has been recognized that the mass and stiffness of the attached nanostrips affect surface-wave resonances to some extent. Here, we reveal the more noticeable influence of the interfacial stiffness between strips and substrate at high frequencies. This influence is confirmed by exciting and detecting surface-wave resonances up to ~ 6 GHz by picosecond ultrasound spectroscopy. The resonance frequency significantly decreases and attenuation increases as the interfacial stiffness decreases for silicon substrate. However, low-attenuation branches appear along the Rayleigh-wave-resonance dispersion curve for silica substrate, and the resonance frequencies remain nearly identical to those of the Rayleigh waves. Previous models fail to reproduce these surface-wave resonance behaviors. The proposed theoretical model, involving the interfacial stiffness, consistently explained them, indicating the importance of the interface bond strength in designing surface-wave resonators. [ABSTRACT FROM AUTHOR]

A ballpoint-pen-type portable ultrasonic oscillator is developed for quantitative measurement of Young's modulus on a solid. It consists of an electrodeless rod-shaped langasite oscillator with a tungsten-carbide spherical-shaped tip at the end, permanent magnets for making a constant force at the contact interface, and antennas for exciting and detecting the longitudinal vibration contactlessly. The resonance frequency of the oscillator is changed by contact with the specimen, reflecting Young's modulus of the specimen at the contact area. The langasite oscillator is supported at the nodal points so that its acoustical contact occurs only at the specimen, making a calibration-free measurement realistic. Young's moduli of various specimens were evaluated within 15% error just by touching the specimens with the probe. The error becomes smaller than 10% for lower Young-modulus materials (<~150GPa). [ABSTRACT FROM AUTHOR]

Heat conduction possesses (thermal) modes in analogy with acoustics even without oscillation. Here, we establish thermal mode spectroscopy to measure the thermal diffusivity of small specimens. Local heating with a light pulse excites such modes that show antinodes at the heating point, and photothermal detection at another antinode spot allows measuring relaxation behavior of the desired mode selectively: The relaxation time yields thermal diffusivity. The Ritz method is proposed for arbitrary geometry specimens. This method is applicable even to a diamond crystal with ∼ mm dimensions. [ABSTRACT FROM AUTHOR]

Oligomer species of amyloid β (Aβ) peptides are intensively investigated because of their relevance to Alzheimer's disease (AD), and a stable oligomer will be a cause of AD. In this article, we investigate the structural stability of two representative Aβ1-40 oligomers, which are with and without the β-sheet structure, denoted by β and non-β oligomers, respectively, using optimized ultrasonic irradiation (OUI). Recent studies reveal that OUI significantly accelerates the fibril formation in Aβ1-40 monomers; it is capable of transforming any unstable oligomers into fibrils (the dead-end products) in a short time. First, we find that β oligomers can be produced under high-speed stirring agitation; their β-sheet structures are evaluated by the circular-dichroism spectrum measurement, by the immunoassay using the fibril-specific OC antibody, and by the seeding experiment, showing identical characteristics to those formed in previous reports. Second, we form non-β oligomers in a high-concentration NaCl solution and confirm that they include no β-sheet structure, and they are recognized by the oligomer-specific A11 antibody. Furthermore, we confirm the neurotoxicity of the two types of oligomers using the neural tissue derived from mouse embryonic stem cells. We apply the OUI agitation to the β and non-β oligomers. The non-β oligomers are transformed into the fibrils, indicating that they are intermediate species in the fibrillation pathway. However, the β oligomers are surprisingly unaffected by OUI, indicating their high thermodynamic stability. We conclude that the β oligomers should be the independent dead-end products of another pathway, different from the fibrillation pathway. [ABSTRACT FROM AUTHOR]

The microtubule (MT) network is highly dynamic and undergoes dramatic reorganizations during the cell cycle. Dimers of α- and β-tubulins rapidly polymerize to and depolymerize from the end of MT fibrils in an intrinsic GTP-dependent manner. MT severing by ATP-driven enzymes such as katanin and spastin contributes significantly to microtubule dynamics, and it has been shown that katanin p60, a AAA+ family protein, has ATPase and MT-severing activities. The mechanism of MT severing by katanin p60 is poorly understood, and the residues in katanin p60 and tubulins important for severing activity were therefore explored in this study. MT-severing activity, but not ATPase activity, was inhibited by mutations of the conserved aromatic residue and the flanking basic residues in the pore region of the katanin p60 hexameric ring. When the acidic residue-rich C-terminal unstructured segment of either α- or β-tubulin was removed, polymerized MTs were resistant to katanin p60 treatment. Interactions between katanin p60 and the mutant MTs, on the other hand, were unaffected. Taken together, these findings led us to propose that the interactions between the positively charged residues of katanin p60 and the acidic tails of both tubulins are essential for efficient severing of MTs. [ABSTRACT FROM AUTHOR]