Wireless sEMG-Based Body-Machine Interface for Assistive Technology Devices.

Assistive technology (AT) tools and appliances are being more and more widely used and developed worldwide to improve the autonomy of people living with disabilities and ease the interaction with their environment. This paper describes an intuitive and wireless surface electromyography (sEMG) based body-machine interface for AT tools. Spinal cord injuries at C5-C8 levels affect patients' arms, forearms, hands, and fingers control. Thus, using classical AT control interfaces (keypads, joysticks, etc.) is often difficult or impossible. The proposed system reads the AT users' residual functional capacities through their sEMG activity, and converts them into appropriate commands using a threshold-based control algorithm. It has proven to be suitable as a control alternative for assistive devices and has been tested with the JACO arm, an articulated assistive device of which the vocation is to help people living with upper-body disabilities in their daily life activities. The wireless prototype, the architecture of which is based on a 3-channel sEMG measurement system and a 915-MHz wireless transceiver built around a low-power microcontroller, uses low-cost off-the-shelf commercial components. The embedded controller is compared with JACO's regular joystick-based interface, using combinations of forearm, pectoral, masseter, and trapeze muscles. The measured index of performance values is 0.88, 0.51, and 0.41 bits/s, respectively, for correlation coefficients with the Fitt's model of 0.75, 0.85, and 0.67. These results demonstrate that the proposed controller offers an attractive alternative to conventional interfaces, such as joystick devices, for upper-body disabled people using ATs such as JACO.

Effect of mechanical deformation on the structure of regenerated Bombyx mori silk fibroin films as revealed using Raman and infrared spectroscopy.

To better understand the effect of mechanical stress during the spinning of silk, the protein orientation and conformation of Bombyx mori regenerated silk fibroin (RSF) films have been studied as a function of deformation in a static mode or in real time by tensile-Raman experiments and polarization modulation infrared linear dichroism (PM-IRLD), respectively. The data show that either for step-by-step or continuous stretching, elongation induces the progressive formation of ß-sheets that align along the drawing axis, in particular above a draw ratio of ~2. The formation of ß-sheets begins before their alignment during a continuous drawing. Unordered chains were, however, never found to be oriented, which explains the very low level of orientation of the amorphous phase of the natural fiber. Stress-perturbed unordered chains readily convert into ß-sheets, the strain-induced transformation following a two-state process. The final level of orientation and ß-sheet content are lower than those found in the native fiber, indicating that various parameters have to be optimized in order to implement a spinning process as efficient as the natural one. Finally, during the stress relaxation period in a step-by-step drawing, there is essentially no change of the content and orientation of the ß-sheets, suggesting that only unordered structures tend to reorganize.

Structure and mechanical properties of spider silk films at the air-water interface.

The kinetics of adsorption of solubilized spider major ampullate (MA) silk fibers at the air-water interface and the molecular structure and mechanical properties of the interfacial films formed have been studied using various physical techniques. The data show that Nephila clavipes MA proteins progressively adsorb at the interface and ultimately form a highly cohesive thin film. In situ infrared spectroscopy shows that as soon as they reach the interface the proteins predominantly form ß sheets. The protein secondary structure does not change significantly as the film grows, and the amount of ß sheet is the same as that of the natural fiber. This suggests that the final ß-sheet content is mainly dictated by the primary structure and not by the underlying formation process. The measure of the shear elastic constant at low strain reveals a very strong, viscous, cohesive assembly. The ß sheets seem to form cross-links dispersed within an intermolecular network, thus probably playing a major role in the film strength. More importantly, the molecular weight seems to be a crucial factor because interfacial films made from the natural proteins are ~7 times stronger and ~3 times more viscous than those obtained previously with shorter recombinant proteins. Brewster angle microscopy at the air-water interface and transmission electron microscopy of transferred films have revealed a homogeneous organization on the micrometer scale. The images suggest that the structural assembly at the air-water interface leads to the formation of macroscopically solid and highly cohesive networks. Overall, the results suggest that natural spider silk proteins, although sharing similarities with recombinant proteins, have the particular ability to self-assemble into ordered materials with exceptional mechanical properties.

Review structure of silk by raman spectromicroscopy: from the spinning glands to the fibers.

Raman spectroscopy has long been proved to be a useful tool to study the conformation of protein-based materials such as silk. Thanks to recent developments, linearly polarized Raman spectromicroscopy has appeared very efficient to characterize the molecular structure of native single silk fibers and spinning dopes because it can provide information relative to the protein secondary structure, molecular orientation, and amino acid composition. This review will describe recent advances in the study of the structure of silk by Raman spectromicroscopy. A particular emphasis is put on the spider dragline and silkworm cocoon threads, other fibers spun by orb-weaving spiders, the spinning dope contained in their silk glands and the effect of mechanical deformation. Taken together, the results of the literature show that Raman spectromicroscopy is particularly efficient to investigate all aspects of silk structure and production. The data provided can lead to a better understanding of the structure of the silk dope, transformations occurring during the spinning process, and structure and mechanical properties of native fibers.

Unexpected differences in the behavior of ovotransferrin at the air-water interface at pH 6.5 and 8.0.

Adsorption of purified apo-ovotransferrin at the air-water interface was studied by ellipsometry, surface tension, polarization-modulation infrared reflection-absorption spectroscopy (PM-IRRAS), and shear elastic constant measurements. No significant difference was observed between pH 6.5 and 8.0 as regards the final value of surface concentration and surface pressure. However at low concentration, a weak barrier to adsorption is evidenced at pH 6.5 and confirmed by PM-IRRAS measurements. At a pH where the protein net charge is negative (pH 8.0), the behavior of ovotransferrin at the air-water interface is more influenced by charge effects rather than bulk concentration effects. At this pH, the interface exhibits a low shear elastic constant and a spectral signature not usual for globular proteins.

Structure and dynamics of cold-adapted enzymes as investigated by FT-IR spectroscopy and MD. The case of an esterase from Pseudoalteromonas haloplanktis.

Psychrophiles are cold-adapted organisms that produce enzymes that display a high catalytic efficiency at low temperatures. In recent years, these low-temperature working enzymes have attracted the attention of scientists because of their peculiar properties that render them particularly useful in investigating the relationship between enzyme stability and flexibility. Recently, a new esterase was identified and isolated from the cold-adapted organism Pseudoalteromonas haloplanktis. The enzyme, denoted as PhEST, presents a dimeric structure with a molecular mass of 60 kDa. In this work, we used Fourier transform infrared spectroscopy and molecular dynamics simulations to investigate the functional and structural properties of PhEST over a wide range of temperature. The obtained results reveal that the structure of PhEST is quite stable up to 40 degrees C. In fact, the protein starts to denature at about 45 degrees C through the formation of new secondary structural elements such as intermolecular beta-sheets. In addition, our results indicate that the flexibility of protein segment 55-65 (335-345 in subunit B), which corresponds to a loop near the active site of the enzyme, plays a crucial role in the protein function.

Surface properties and conformation of Nephila clavipes spider recombinant silk proteins at the air-water interface.

The dragline fiber of spiders is composed of two proteins, the major ampullate spidroins I and II (MaSpI and MaSpII). To better understand the assembly mechanism and the properties of these proteins, the adsorption behavior of the recombinant proteins of the spider Nephila clavipes produced by Nexia Biotechnologies Inc. has been studied at the air-water interface using ellipsometry, surface pressure, rheological, and infrared measurements. The results show that the adsorption is more rapid and more molecules are present at the interface for MaSpII than for MaSpI. MaSpII has thus a higher affinity for the interface than MaSpI, which is consistent with its higher aggregation propensity in water. The films formed at the interface consist of networks containing a high content of intermolecular beta-sheets as revealed by the in situ polarization modulation infrared absorption reflection spectra. The infrared results further demonstrate that, for MaSpI, the beta-sheets are formed as soon as the proteins adsorb to the interface while for MaSpII the beta-sheet formation occurs more slowly. The amount of beta-sheets is lower for MaSpII than for MaSpI, most likely due to the presence of proline residues in its sequence. Both proteins form elastic films, but they are heterogeneous for MaSpI and homogeneous for MaSpII most probably as a result of a more ordered and slower aggregation process for MaSpII. This difference in their mechanism of assembly and interfacial behaviors does not seem to arise from their overall hydrophobicity or from a specific pattern of hydrophobicity, but rather from the longer polyalanine motifs, lower glycine content, and higher proline content of MaSpII. The propensity of both spidroins to form beta-sheets, especially the polyalanine blocks, suggests the participation of both proteins in the silk's beta-sheet crystallites.

In situ conformation of spider silk proteins in the intact major ampullate gland and in solution.

To understand the spinning process of dragline silk by spiders, the protein conformation before spinning has to be determined. Raman confocal spectromicroscopy has been used to study the conformation of the proteins in situ in the intact abdominal major ampullate gland of Nephila clavipes and Araneus diadematus spiders. The spectra obtained are typical of natively unfolded proteins and are very similar to that of a mixture of recombinant silk proteins. Vibrational circular dichroism reveals that the conformation is composed of random and polyproline II (PPII) segments with some alpha-helices. The alpha-helices seem to be located in the C-terminal part whereas the repetitive sequence is unfolded. The PPII structure can significantly contribute to the efficiency of the spinning process in nature.