Calligraphic interdigitated capacitive sensors for green electronics.

This study presents a novel approach to fabricating interdigitated capacitive (IDC) touch sensors using graphite-based pencils on a wood substrate. The sensors were designed to detect touches and pressure variations, offering a cost-effective and environmentally friendly solution for sensor fabrication. The fabrication process involved abrasion of graphite pencils on a wooden substrate to create conductive traces, followed by the integration of interdigitated electrode structures. Capacitance variations resulting from touch interactions were investigated to calibrate sensor responses for tailored tasks. The sensitivity of the sensor was found to be 1.2 pF/kPa, highlighting its responsiveness to pressure variations. Additionally, the sensors were interfaced with an Arduino Uno microcontroller board to demonstrate practical applications, such as replicating arrow key functionality. Additionally, the sensors exhibit sensitivity to environmental factors, with the relative change in capacitance increasing from 0.1 to 0.65 as relative humidity ranges from 30 to 90%. Furthermore, variations in temperature from 30 to 60ºC result in a relative change in capacitance increasing to approximately 0.5. The results indicate the feasibility and versatility of using wood-based substrates and graphite-based pencils for fabricating IDC touch sensors, offering promising prospects for sustainable and accessible sensor technology.

Strategies To Modify the Surface and Bulk Properties of 3D-Printed Solid Scaffolds for Tissue Engineering Applications.

3D printing is one of the effective scaffold fabrication techniques that emerged in the 21st century that has the potential to revolutionize the field of tissue engineering. The solid scaffolds developed by 3D printing are still one of the most sought-after approaches for developing hard-tissue regeneration and repair. However, applications of these solid scaffolds get limited due to their poor surface and bulk properties, which play a significant role in tissue integration, loadbearing, antimicrobial/antifouling properties, and others. As a result, several efforts have been directed to modify the surface and bulk of these solid scaffolds. These modifications have significantly improved the adoption of 3D-printed solid scaffolds and devices in the healthcare industry. Nevertheless, the in vivo implant applications of these 3D-printed solid scaffolds/devices are still under development. They require attention in terms of their surface/bulk properties, which dictate their functionality. Therefore, in the current review, we have discussed different 3D-printing parameters that facilitate the fabrication of solid scaffolds/devices with different properties. Further, changes in the bulk properties through material and microstructure modification are also being discussed. After that, we deliberated on the techniques that modify the surfaces through chemical and material modifications. The computational approaches for the bulk modification of these 3D-printed materials are also mentioned, focusing on tissue engineering. We have also briefly discussed the application of these solid scaffolds/devices in tissue engineering. Eventually, the review is concluded with an analysis of the choice of surface/bulk modification based on the intended application in tissue engineering.

Local and non-local topological information in the denatured state ensemble of a ß-barrel protein.

The folding of predominantly ß-sheet proteins is complicated by the presence of a large number of non-local interactions in their native states, which increase the ruggedness of their folding energy landscapes. However, forming non-local contacts early in folding or even in the unfolded state can smooth the energy landscape and facilitate productive folding. We report that several sequence regions of a ß-barrel protein, cellular retinoic acid-binding protein 1 (CRABP1), populate native-like secondary structure to a significant extent in the denatured state in 8 M urea. In addition, we provide evidence for both local and non-local interactions in the denatured state of CRABP1. NMR chemical shift perturbations (CSPs) under denaturing conditions upon substitution of single residues by mutation support the presence of several non-local interactions in topologically key sites, arguing that the denatured state is conformationally restricted and contains topological information for the native fold. Among the most striking non-local interactions are those between the N- and C-terminal regions, which are involved in closure of the native ß-barrel. In addition, CSPs support the presence of two features in the denatured state: a major hydrophobic cluster involving residues from various parts of the sequence and a native-like interaction similar to one identified in previous studies as forming early in folding (Budyak et al., Structure 21, 476 [2013]). Taken together, our data support a model in which transient structures involving nonlocal interactions prime early folding interactions in CRABP1, determine its barrel topology, and may protect this predominantly ß-sheet protein against aggregation.

Safety, sterility and stability of direct-from-vial multiple dosing intravitreal injection of bevacizumab.

BACKGROUND: This study aims to determine the stability, sterility and safety of bevacizumab multiple dosing from a single vial without prior aliquoting. METHODS: In-vitro and human study. Six bevacizumab vials, used in multiple patients on a single day by direct withdrawal from the vial, and stored in 4°C up to a variable period, were tested for stability (high-performance liquid chromatography; [HPLC]), sterility (culture), conformational stability by circular dichroism and fluorescence spectroscopy and the rubber cork structural integrity (electron microscopy [EM]). RESULTS: HPLC of all six samples of used bevacizumab and the control bevacizumab sample were similar; culture was negative; and the EM of rubber corks did not show an open communication. Spectroscopic studies indicated drug conformational stability. Further, there was no infection or inflammation in 221 consecutive patients (973 injections) when bevacizumab was stored at 4°C and used for one week. CONCLUSION: Bevacizumab does not lose stability when stored at 4°C. It may be used for a week by direct withdrawal from the vial without fear of infection or inflammation if all standard precautions related to intravitreal injection are adhered to.

Copper alters aggregation behavior of prion protein and induces novel interactions between its N- and C-terminal regions.

Copper is reported to promote and prevent aggregation of prion protein. Conformational and functional consequences of Cu(2+)-binding to prion protein (PrP) are not well understood largely because most of the Cu(2+)-binding studies have been performed on fragments and truncated variants of the prion protein. In this context, we set out to investigate the conformational consequences of Cu(2+)-binding to full-length prion protein (PrP) by isothermal calorimetry, NMR, and small angle x-ray scattering. In this study, we report altered aggregation behavior of full-length PrP upon binding to Cu(2+). At physiological temperature, Cu(2+) did not promote aggregation suggesting that Cu(2+) may not play a role in the aggregation of PrP at physiological temperature (37 °C). However, Cu(2+)-bound PrP aggregated at lower temperatures. This temperature-dependent process is reversible. Our results show two novel intra-protein interactions upon Cu(2+)-binding. The N-terminal region (residues 90-120 that contain the site His-96/His-111) becomes proximal to helix-1 (residues 144-147) and its nearby loop region (residues 139-143), which may be important in preventing amyloid fibril formation in the presence of Cu(2+). In addition, we observed another novel interaction between the N-terminal region comprising the octapeptide repeats (residues 60-91) and helix-2 (residues 174-185) of PrP. Small angle x-ray scattering studies of full-length PrP show significant compactness upon Cu(2+)-binding. Our results demonstrate novel long range inter-domain interactions of the N- and C-terminal regions of PrP upon Cu(2+)-binding, which might have physiological significance.

Drying of 'Perlette' grape under different physical treatment for raisin making.

Experiments were conducted to evaluate the suitability of grape (Vitis vinifera L) cv. 'Perlette' for raisin preparation with different physical treatments. The treatments consisted of whole berries, half cut berries and berries with superficial abrasion of peel/waxy cuticle. The effectiveness of these treatments on drying characteristics and quality of the prepared raisin were studied. The half cut berries took less time to dry as compared to scratchy surfaced berries and whole berries. Drying of berries was carried out at 60 °C in an air circulatory tray dryer with loading capacity of 6.0 kg/m(2). Initial moisture content of berries was 67% (wb) with varying total soluble solids of 15-18% which was dried to moisture content of around 15% (wb). Empirical/semi-theoretical/mathematical models, commonly describing thin-layer drying of various biological materials have been investigated to illustrate the drying characteristics of the physically treated berries. A non-linear regression analysis using a standard statistical program was used to evaluate the constants of mathematical models to describe appropriately the drying behaviour. The results as indicated that the abrasion method is effective for faster drying as against the chemical method; however this treatment gave comparatively darker raisin which was less attractive.

UV-light exposed prion protein fails to form amyloid fibrils.

Amyloid fibril formation involves three steps; structural perturbation, nucleation and elongation. We have investigated amyloidogenesis using prion protein as a model system and UV-light as a structural perturbant. We find that UV-exposed prion protein fails to form amyloid fibrils. Interestingly, if provided with pre-formed fibrils as seeds, UV-exposed prion protein formed amyloid fibrils albeit with slightly different morphology. Atomic force microscopy and electron microscopic studies clearly show the formation of fibrils under these conditions. Circular dichroism study shows loss in helicity in UV-exposed protein. UV-exposed prion protein fails to form amyloid fibrils. However, it remains competent for fibril extension, suggesting that UV-exposure results in loss of nucleating capability. This work opens up possibility of segregating nucleation and elongation step of amyloidogenesis, facilitating screening of new drug candidates for specifically inhibiting either of these processes. In addition, the work also highlights the importance of light-induced structural and functional alterations which are important in protein based therapeutics.