The extracellular matrix integrates mitochondrial homeostasis.

Cellular homeostasis is intricately influenced by stimuli from the microenvironment, including signaling molecules, metabolites, and pathogens. Functioning as a signaling hub within the cell, mitochondria integrate information from various intracellular compartments to regulate cellular signaling and metabolism. Multiple studies have shown that mitochondria may respond to various extracellular signaling events. However, it is less clear how changes in the extracellular matrix (ECM) can impact mitochondrial homeostasis to regulate animal physiology. We find that ECM remodeling alters mitochondrial homeostasis in an evolutionarily conserved manner. Mechanistically, ECM remodeling triggers a TGF-ß response to induce mitochondrial fission and the unfolded protein response of the mitochondria (UPRMT). At the organismal level, ECM remodeling promotes defense of animals against pathogens through enhanced mitochondrial stress responses. We postulate that this ECM-mitochondria crosstalk represents an ancient immune pathway, which detects infection- or mechanical-stress-induced ECM damage, thereby initiating adaptive mitochondria-based immune and metabolic responses.

Thickness-dependent carrier transport of PdSe2films grown by plasma-assisted metal selenization.

Atomically thin narrow-bandgap layered PdSe2has attracted much attention due to its rich and unique electrical properties. For silicon-compatible device integration, direct wafer-scale preparation of high-quality PdSe2thin film on a silicon substrate is highly desired. Here, we present the low-temperature synthesis of large-area polycrystalline PdSe2films grown on SiO2/Si substrates by plasma-assisted metal selenization and investigate their charge carrier transport behaviors. Raman analysis, depth-dependent x-ray photoelectron spectroscopy, and cross-sectional transmission electron microscopy were used to reveal the selenization process. The results indicate a structural evolution from initial Pd to intermediate PdSe2-xphase and eventually to PdSe2. The field-effect transistors fabricated from these ultrathin PdSe2films exhibit strong thickness-dependent transport behaviors. For thinner films (4.5 nm), a record high on/off ratio of 104was obtained. While for thick ones (11 nm), the maximum hole mobility is about 0.93 cm2V-1S-1, which is the record high value ever reported for polycrystalline films. These findings suggest that our low-temperature-metal-selenized PdSe2films have high quality and show great potential for applications in electrical devices.

Effects of Externally Applied Electric Fields on the Manipulation of Solvated-Chignolin Folding: Static- versus Alternating-Field Dichotomy at Play.

The interaction between a protein and external electric field (EF) can alter its structure and dynamical behavior, which has a potential impact on the biological function of proteins and cause uncertain health consequences. Conversely, the application of EFs of judiciously selected intensity and frequency can help to treat disease, and optimization of this requires a greater understanding of EF-induced effects underpinning basic protein biophysics. In the present study, chignolin─an artificial protein sufficiently small to undergo fast-folding events and transitions─was selected as an ideal prototype to investigate how, and to what extent, externally applied electric fields may manipulate or influence protein-folding phenomena. Nonequilibrium molecular dynamics (NEMD) simulations have been performed of solvated chignolin to determine the distribution of folding states and their underlying transition dynamics, in the absence and presence of externally applied electric fields (both static and alternating); a key focus has been to ascertain how folding pathways are altered in an athermal sense by external fields. Compared to zero-field conditions, a dramatically different─indeed, bifurcated─behavior of chignolin-folding processes emerges between static- and alternating-field scenarios, especially vis-à-vis incipient stages of hydrophobic-core formation: in alternating fields, fold-state populations diversified, with an attendant acceleration of state-hopping folding kinetics, featuring the concomitant emergence of a new, quasi-stable structure compared to the native structure, in field-shifted energy landscapes.

Investigation of Dipolar Response of the Hydrated Hen-Egg White Lysozyme Complex under Externally Applied Electric Fields: Insights from Non-equilibrium Molecular Dynamics.

Given its ubiquitous presence in the environment of bio-macromolecules, water is well known to play a fundamental part in biological activity, often as a regulating agent. In parallel, with increasing attention focused on the potential damage of microwave-frequency radiation exposure to human health, the effects of extraneous electric and electromagnetic (e/m) fields on water shells surrounding proteins, and, indeed, biomolecules themselves, are becoming a particularly pertinent issue. In this study, non-equilibrium molecular dynamics simulations of hydrated hen-egg white lysozyme have been performed in both the absence and presence of external electric fields of varying intensity (0.005-0.02 V/Å) and frequency (static, i.e., zero-frequency, together with oscillating fields of 2.45-100 GHz). By comparing the effect of different electric-field conditions on both the protein's and surrounding hydration layer's dipole moments and their underlying relaxation dynamics, clear and evident non-thermal field effects were observed on the dipolar response of both the protein and hydration layer. This occurred primarily as a consequence of the protein's dipolar alignment with the external field and increased with the growth of field intensity. In addition, it was found that the lag time of dipolar response to the applied field itself, for both the protein and the first hydration sub-shell (i.e., directly adsorbed layer), under oscillating fields is longer than that in both the second hydration sub-layer and bulk water, owing to strong direct protein-water adsorption. In that respect, we also probe and discuss the effect of protein-water hydrogen bonds, dissecting the subtleties of "bio-water" dipolar response.