Folding State Research Articles

Ethanolamine-modified gel electrolyte of zinc ion battery

The rapid growth of wearable electronic devices has spurred the development of flexible energy storage systems. However, the limitations of conventional rigid commercial batteries have hindered the advancement of wearable technology. Consequently, the development of stable, safe, highly flexible, and cost-effective flexible batteries has become a key focus in current battery research. Herein, we introduce a novel multifunctional flexible Prussian Blue–zinc battery utilizing a PVA-ZnCl₂ polymer gel electrolyte (EGPE) enhanced with ethanolamine (ETA), aimed at addressing the deficiencies of traditional electrolytes in terms of safety and mechanical performance. The Zn||Zn symmetric cell using EGPE electrolyte demonstrated an impressive long-term cycling stability of over 3000 hours at a current density of 0.15 mA cm−2. In contrast, the symmetrical cell using 0.8 M ZnCl2 aqueous electrolyte maintained its stability for only 400 hours. In addition, the prepared flexible zinc Prussian blue device maintained more than 65 % of its initial capacity of the device and its coulombic efficiency was close to 100 % after 400 cycles at an extreme current density of 10 A g−1. Furthermore, flexible device using the EGPE was able to maintain a stable power supply under various bending, torsion, folding and shearing conditions. Such innovative gel electrolyte demonstrated considerable prospects for utilisation in portably equipped devices and energy storage systems.

Origami inspired dual matrix intelligent shape memory polymer composite folds for deployable structures

Abstract It remains a challenge to develop an intelligent, programmable multifunctional material system capable of recovering shape, withstanding high loads, and detecting folding extent remotely for self-deployable structures used in aerospace, robotics, and medical devices. In this work, our objective is to develop intelligent shape memory polymer composite (iSMPC) folds embedded with reduced graphene oxide (rGO)-coated self-sensing fabric. This will enable remote sensing of the fold state based on resistance changes and achieve higher strength and modulus. Firstly, we demonstrate the ability to sense the extent of folding and establish the relationship between piezoresistivity and fold state change by conducting cyclic compression analysis on folds with different gap sizes (6mm, 9mm, and 12mm) at temperatures of 25°C, 35°C, and 45°C. The iSMPC fold with a 6mm gap exhibited the highest bending stiffness (650.3Nmm-1) and curvature (0.55mm-1), resulting in a higher change in fractional change in resistance (FCR). Subsequently, the shape memory cycles of the 6mm iSMPC fold were demonstrated through localized controlled heating. Its shape recovery process exhibited repeatable behavior with a high recovery ratio of 95%. Lastly, a two-fold iSMPC structure was developed, and its performance was analyzed during a complete shape memory cycle. The piezoresistive response during higher-temperature cyclic loading resembled that of the single fold, exhibiting an FCR range between -9% and 5%, thereby demonstrating the repeatability of the iSMPC fold response.

A Multimodal Perception-Enabled Flexible Memristor with Combined Sensing-Storage-Memory Functions for Enhanced Artificial Injury Recognition.

With the continuous advancement of wearable technology and advanced medical monitoring, there is an increasing demand for electronic devices that can adapt to complex environments and have high perceptual sensitivity. Here, a novel artificial injury perception device based on an Ag/HfOx/ITO/PET flexible memristor is designed to address the limitations of current technologies in multimodal perception and environmental adaptability. The memristor exhibits excellent resistive switching (RS) performance and mechanical flexibility under different bending angles (BAs), temperatures, humid environment, and repetitive folding conditions. Further, the device demonstrates the multimodal perception and conversion capabilities toward voltage, mechanical, and thermal stimuli through current response tests under different conditions, enabling not only the simulation of artificial injury perception but also holds promise for monitoring and controlling the movement of robotic arms. Moreover, the logical operation capability of the memristor-based reconfigurable logic (MRL) gates is also demonstrated, proving the device has great potential applications with sensing, storage, and memory functions. Overall, this study not only provides a direction for the development of the next-generation flexible multimodal sensors, but also has significant implications for technological advancements in many fields such as robotic arms, electronic skin (e-skin), and medical monitoring.

Acoustic Character Governing Variation in Normal, Benign, and Malignant Voices.

Benign and malignant vocal fold lesions (VFLs) are growths that occur on the vocal folds. However, the treatments for these two types of lesions differ significantly. Therefore, it is imperative to use a multidisciplinary approach to properly recognize suspicious lesions. This study aimed to determine the important acoustic characteristics specific to benign and malignant VFLs. The acoustic model of voice quality was utilized to measure various acoustic parameters in 157 participants, including individuals with normal, benign, and malignant conditions. The study comprised 62 female and 95 male participants (43 ± 10 years). Voice samples were collected at the Shanghai Eye, Ear, Nose, and Throat Hospital of Fudan University between May 2020 and July 2021. The acoustic variables of the participants were analyzed using Principal Component Analysis (PCA) to present important acoustic characteristics that are specific to normal vocal folds, benign VFLs, and malignant VFLs. The similarities and differences in acoustic factors were also studied for benign conditions including Reinke's edema, polyps, cysts, and leukoplakia. Using the PCA method, the components that accounted for the variation in the data were identified, highlighting acoustic characteristics in the normal, benign, and malignant groups. The analysis indicated that coefficients of variation in root mean square energy were observed solely within the normal group. Coefficients of variation in pitch (F0) were found to be significant only in benign voices, while higher formant frequencies and their variability were identified as contributors to the acoustic variance within the malignant group. The presence of formant dispersion (FD) as a weighted factor in PCA was exclusively noted in individuals with Reinke's edema. The amplitude ratio between subharmonics and harmonics (SHR) and its coefficients of variation were evident exclusively in the polyps group. In the case of voices with cysts, both pitch (F0) and coefficients of variation for FD were observed to contribute to variations. Additionally, higher formant frequencies and their coefficients of variation played a role in the acoustic variance among voices of patients with leukoplakia. Experimental evidence demonstrates the utility of the PCA method in the identification of vibrational alterations in the acoustic characteristics of voice affected by lesions. Furthermore, the PCA analysis has highlighted underlying acoustic differences between various conditions such as Reinke's edema, polyps, cysts, and leukoplakia. These findings can be used in the future to develop an automated malignant voice analysis algorithm, which will facilitate timely intervention and management of vocal fold conditions.

Stabilization of Non-Native Folds and Programmable Protein Gelation in Compositionally Designed Deep Eutectic Solvents.

Proteins are adjustable units from which biomaterials with designed properties can be developed. However, non-native folded states with controlled topologies are hardly accessible in aqueous environments, limiting their prospects as building blocks. Here, we demonstrate the ability of a series of anhydrous deep eutectic solvents (DESs) to precisely control the conformational landscape of proteins. We reveal that systematic variations in the chemical composition of binary and ternary DESs dictate the stabilization of a wide range of conformations, that is, compact globular folds, intermediate folding states, or unfolded chains, as well as controlling their collective behavior. Besides, different conformational states can be visited by simply adjusting the composition of ternary DESs, allowing for the refolding of unfolded states and vice versa. Notably, we show that these intermediates can trigger the formation of supramolecular gels, also known as eutectogels, where their mechanical properties correlate to the folding state of the protein. Given the inherent vulnerability of proteins outside the native fold in aqueous environments, our findings highlight DESs as tailorable solvents capable of stabilizing various non-native conformations on demand through solvent design.

Recruitment of Ahsa1 to Hsp90 is regulated by a conserved peptide that inhibits ATPase stimulation

Hsp90 is a molecular chaperone that acts on its clients through an ATP-dependent and conformationally dynamic functional cycle. The cochaperone Accelerator of Hsp90 ATPase, or Ahsa1, is the most potent stimulator of Hsp90 ATPase activity. Ahsa1 stimulates the rate of Hsp90 ATPase activity through a conserved motif, NxNNWHW. Metazoan Ahsa1, but not yeast, possesses an additional 20 amino acid peptide preceding the NxNNWHW motif that we have called the intrinsic chaperone domain (ICD). The ICD of Ahsa1 diminishes Hsp90 ATPase stimulation by interfering with the function of the NxNNWHW motif. Furthermore, the NxNNWHW modulates Hsp90’s apparent affinity to Ahsa1 and ATP. Lastly, the ICD controls the regulated recruitment of Hsp90 in cells and its deletion results in the loss of interaction with Hsp90 and the glucocorticoid receptor. This work provides clues to how Ahsa1 conserved regions modulate Hsp90 kinetics and how they may be coupled to client folding status.

Characterization of βB2-crystallin tryptophan mutants reveals two different folding states in solution.

Conserved tryptophan residues are critical for the structure and the stability of β/γ-crystallin in the lenses of vertebrates. During aging, in which the lenses are continuously exposed to ultraviolet irradiation and other environmental stresses, oxidation of tryptophan residues in β/γ-crystallin is triggered and impacts the lens proteins to varying degrees. Kynurenine derivatives, formed by oxidation of tryptophan, accumulate, resulting in destabilization and insolubilization of β/γ-crystallin, which correlates with age-related cataract formation. To understand the contribution of tryptophan modification on the structure and stability of human βB2-crystallin, five tryptophan residues were mutated to phenylalanine considering its similarity in structure and hydrophilicity to kynurenine. Among all mutants, W59F and W151F altered the stability and homo-oligomerization of βB2-crystallin-W59F promoted tetramerization whereas W151F blocked oligomerization. Most W59F dimers transformed into tetramer in a month, and the separated dimer and tetramer of W59F demonstrated different structures and hydrophobicity, implying that the biochemical properties of βB2-crystallin vary over time. By using SAXS, we found that the dimer of βB2-crystallin in solution resembled the lattice βB1-crystallin dimer (face-en-face), whereas the tetramer of βB2-crystallin in solution resembled its lattice tetramer (domain-swapped). Our results suggest that homo-oligomerization of βB2-crystallin includes potential inter-subunit reactions, such as dissociation, unfolding, and re-formation of the dimers into a tetramer in solution. The W>F mutants are useful in studying different folding states of βB2-crystallin in lens.

A Stochastic Landscape Approach for Protein Folding State Classification.

Protein folding is a critical process that determines the functional state of proteins. Proper folding is essential for proteins to acquire their functional three-dimensional structures and execute their biological role, whereas misfolded proteins can lead to various diseases, including neurodegenerative disorders like Alzheimer's and Parkinson's. Therefore, a deeper understanding of protein folding is vital for understanding disease mechanisms and developing therapeutic strategies. This study introduces the Stochastic Landscape Classification (SLC), an innovative, automated, nonlearning algorithm that quantitatively analyzes protein folding dynamics. Focusing on collective variables (CVs) - low-dimensional representations of complex dynamical systems like molecular dynamics (MD) of macromolecules - the SLC approach segments the CVs into distinct macrostates, revealing the protein folding pathway explored by MD simulations. The segmentation is achieved by analyzing changes in CV trends and clustering these segments using a standard density-based spatial clustering of applications with noise (DBSCAN) scheme. Applied to the MD-based CV trajectories of Chignolin and Trp-Cage proteins, the SLC demonstrates apposite accuracy, validated by comparing standard classification metrics against ground-truth data. These metrics affirm the efficacy of the SLC in capturing intricate protein dynamics and offer a method to evaluate and select the most informative CVs. The practical application of this technique lies in its ability to provide a detailed, quantitative description of protein folding processes, with significant implications for understanding and manipulating protein behavior in industrial and pharmaceutical contexts.

Fluorescein-Based SynNotch Adaptors for Regulating Gene Expression Responses to Diverse Extracellular Cues.

We introduce an adaptor-based strategy for regulating fluorescein-binding synthetic Notch (SynNotch) receptors using ligands based on conjugates of fluorescein isomers and analogs. To develop a versatile system, we evaluated the surface expression and activities of multiple constructs containing distinct extracellular fluorescein-binding domains. Using an optimized receptor, we devised ways to regulate signaling via fluorescein-based chemical transformations, including an approach based on a bio-orthogonal chemical ligation and a spatially controllable strategy via the photo-patterned uncaging of an o -nitrobenzyl-caged fluorescein conjugate. We further demonstrate that fluorescein-conjugated extracellular matrix (ECM)-binding peptides can regulate SynNotch activity depending on the folding state of collagen-based ECM networks. Treatment with these conjugates enabled cells to distinguish between folded versus denatured collagen proteins and enact dose-dependent gene expression responses depending on the nature of the signaling adaptors presented. To demonstrate the utility of these tools, we applied them to control the myogenic conversion of fibroblasts into myocytes with spatial and temporal precision and in response to denatured collagen-I, a biomarker of multiple pathological states. Overall, we introduce an optimized fluorescein-binding SynNotch as a versatile tool for regulating transcriptional responses to extracellular ligands based on the widely used and clinically-approved fluorescein dye.

Dolphin CONTINUE: a multi-center randomized controlled trial to assess the effect of a nutritional intervention on brain development and long-term outcome in infants born before 30 weeks of gestation

BackgroundPreterm born infants are at risk for brain injury and subsequent developmental delay. Treatment options are limited, but optimizing postnatal nutrition may improve brain- and neurodevelopment in these infants. In pre-clinical animal models, combined supplementation of docosahexaenoic acid (DHA), choline, and uridine-5-monophosphate (UMP) have shown to support neuronal membrane formation. In two randomized controlled pilot trials, supplementation with the investigational product was associated with clinically meaningful improvements in cognitive, attention, and language scores. The present study aims to assess the effect of a similar nutritional intervention on brain development and subsequent neurodevelopmental outcome in infants born very and extremely preterm.MethodsThis is a randomized, placebo-controlled, double-blinded, parallel-group, multi-center trial. A total of 130 infants, born at less than 30 weeks of gestation, will be randomized to receive a test or control product between term-equivalent age and 12 months corrected age (CA). The test product is a nutrient blend containing DHA, choline, and UMP amongst others. The control product contains only fractions of the active components. Both products are isocaloric powder supplements which can be added to milk and solid feeds. The primary outcome parameter is white matter integrity at three months CA, assessed using diffusion-tensor imaging (DTI) on MRI scanning. Secondary outcome parameters include volumetric brain development, cortical thickness, cortical folding, the metabolic and biochemical status of the brain, and product safety. Additionally, language, cognitive, motor, and behavioral development will be assessed at 12 and 24 months CA, using the Bayley Scales of Infant Development III and digital questionnaires (Dutch version of the Communicative Development Inventories (N-CDI), Ages and Stages Questionnaire 4 (ASQ-4), and Parent Report of Children’s Abilities – Revised (PARCA-R)).DiscussionThe investigated nutritional intervention is hypothesized to promote brain development and subsequent neurodevelopmental outcome in preterm born infants who have an inherent risk of developmental delay. Moreover, this innovative study may give rise to new treatment possibilities and improvements in routine clinical care.Trial registrationWHO International Clinical Trials Registry: NL-OMON56181 (registration assigned October 28, 2021).

Analytical Aspects of ANSA-BSA Association: A Thermodynamic and Conformational Approach.

Many studies have demonstrated the manner in which ANS interacts with bovine serum albumin (BSA), although they are limited by the extremely low solubility of dye. The present study demonstrates the binding of ANSA dye with BSA, and since this dye can easily replace ANS, it not only simplifies research but also improves sensor accuracy for serum albumin. A combination of calorimetry and spectroscopy has been employed to establish the thermodynamic signatures associated with the interaction of ANSA with the protein and the consequent conformational changes in the latter. The results of differential scanning calorimetry reveal that when the concentration of ANSA in solution is increased, the thermal stability of the protein increases substantially. The fluorescence data demonstrated a decrease in the binding affinity of ANSA with the protein when pH increased but was unable to identify a change in the mode of interaction of the ligand. ITC has demonstrated that the mode of interaction between ANSA and the protein varies from a single set of binding sites at pH 5 and 7.4 to a sequential binding site at pH 10, emphasizing the potential relevance of protein conformational changes. TCSPC experiments suggested a dynamic type in the presence of ANSA. Molecular docking studies suggest that ANSA molecules are able to find ionic centers in the hydrophobic pockets of BSA. The findings further imply that given its ease of use in experiments, ANSA may be a useful probe for tracking the presence of serum albumin and partially folded protein states.

Protein Editing using a Concerted Transposition Reaction.

Protein engineering through the chemical or enzymatic ligation of polypeptide fragments has proven enormously powerful for studying countless biochemical processes in vitro. In general, this strategy necessitates a protein folding step following ligation of the unstructured fragments, a requirement that constrains the types of systems amenable to the approach. Here, we report an in vitro strategy that allows internal regions of target proteins to be replaced in a single operation. Conceptually, our system is analogous to a DNA transposition reaction, but employs orthogonal pairs of split inteins to swap out a designated region of a host protein with an exogenous molecular cassette. We show using isotopic labeling experiments that this 'protein transposition' reaction is concerted when the kinetics for the embedded intein pairs are suitably matched. Critically, this feature allows for efficient manipulation of protein primary structure in the context of a native fold. The utility of this method is illustrated using several protein systems including the multisubunit chromatin remodeling complex, ACF, where we also show protein transposition can occur in situ within the cell nucleus. By carrying out a molecular 'cut and paste' on a protein or protein complex under native folding conditions, our approach dramatically expands the scope of protein semisynthesis.

Microbial aromatic amino acid metabolism is modifiable in fermented food matrices to promote bioactivity

Ingestion of fermented foods impacts human immune function, yet the bioactive food components underlying these effects are not understood. Here, we interrogated whether fermented food bioactivity relates to microbial metabolites derived from aromatic amino acids, termed aryl-lactates. Using targeted metabolomics, we established the presence of aryl-lactates in commercially available fermented foods. After pinpointing fermented food-associated lactic acid bacteria that produce high levels of aryl-lactates, we identified fermentation conditions to increase aryl-lactate production in food matrices up to 5 × 103 fold vs. standard fermentation conditions. Using ex vivo reporter assays, we found that food matrix conditions optimized for aryl-lactate production exhibited enhanced agonist activity for the human aryl-hydrocarbon receptor (AhR) as compared to standard fermentation conditions and commercial products. Reduced microbial-induced AhR activity has emerged as a hallmark of many chronic inflammatory diseases, thus we envision strategies to enhance AhR bioactivity of fermented foods to be leveraged to improve human health.

Capture dynamics and driving method of origami capture mechanism in orbit

This article focuses on the dynamic problem of origami capture mechanism capturing space debris in orbit. It delves into the envelope characteristics of the origami capture mechanism, analyzing the motion laws of its axisymmetric folding state. Furthermore, it establishes a kinematic model for the axisymmetric envelope of the origami capture mechanism. A rigid body dynamic model of the origami capture mechanism and a generalized torque equation for the hinge at the crease were established based on the D–H parameter method and the Lagrange method. The enveloping process of the origami capture mechanism in the microgravity environment was simulated using ADAMS software, and the accuracy of the rigid body dynamics model of the origami capture mechanism and the generalized moment equation of the hinge at the crease was verified. Using Ls-Dyna software to simulate the capture process of space debris by force-driven and displacement-driven flexible origami capture mechanisms in microgravity environments, the results show that displacement-driven origami capture mechanisms can quickly capture space debris and are suitable for capturing large-sized space debris; The force-driven origami capture mechanism can quickly complete envelope capture of space debris, suitable for capturing small-sized space debris.

Not All Binding Sites Are Equal: Site Determination and Folding State Analysis of Gas-Phase Protein-Metallodrug Adducts.

Modern approaches in metallodrug research focus on compounds that bind protein targets rather than DNA. However, the identification of protein targets and binding sites is challenging. Using intact mass spectrometry and proteomics, we investigated the binding of the antimetastatic agent RAPTA-C to the model proteins ubiquitin, cytochrome c, lysozyme, and myoglobin. Binding to cytochrome c and lysozyme was negligible. However, ubiquitin bound up to three Ru moieties, two of which were localized at Met1 and His68 as [Ru(cym)], and [Ru(cym)] or [Ru(cym)(PTA)] adducts, respectively. Myoglobin bound up to four [Ru(cym)(PTA)] moieties and five sites were identified at His24, His36, His64, His81/82 and His113. Collision-induced unfolding (CIU) studies via ion-mobility mass spectrometry allowed measuring protein folding as a function of collisional activation. CIU of protein-RAPTA-C adducts showed binding of [Ru(cym)] to Met1 caused a significant compaction of ubiquitin, likely from N-terminal S-Ru-N chelation, while binding of [Ru(cym)(PTA)] to His residues of ubiquitin or myoglobin induced a smaller effect. Interestingly, the folded state of ubiquitin formed by His functionalization was more stable than Met1 metalation. The data suggests that selective metalation of amino acids at different positions on the protein impacts the conformation and potentially the biological activity of anticancer compounds.

Systematic Investigation of the Trafficking of Glycoproteins on the Cell Surface

Glycoproteins located on the cell surface play a pivotal role in nearly every extracellular activity. N-glycosylation is one of the most common and important protein modifications in eukaryotic cells, and it often regulates protein folding and trafficking. Glycosylation of cell-surface proteins undergoes meticulous regulation by various enzymes in the endoplasmic reticulum (ER) and the Golgi, ensuring their proper folding and trafficking to the cell surface. However, the impacts of protein N-glycosylation, N-glycan maturity, and protein folding status on the trafficking of cell-surface glycoproteins remain to be explored. In this work, we comprehensively and site-specifically studied the trafficking of cell-surface glycoproteins in human cells. Integrating metabolic labeling, bioorthogonal chemistry, and multiplexed proteomics, we investigated 706 N-glycosylation sites on 396 cell-surface glycoproteins in monocytes, either by inhibiting protein N-glycosylation, disturbing N-glycan maturation, or perturbing protein folding in the ER. The current results reveal their distinct impacts on the trafficking of surface glycoproteins. The inhibition of protein N-glycosylation dramatically suppresses the trafficking of many cell-surface glycoproteins. The N-glycan immaturity has more substantial effects on proteins with high N-glycosylation site densities, while the perturbation of protein folding in the ER exerts a more pronounced impact on surface glycoproteins with larger sizes. Furthermore, for N-glycosylated proteins, their trafficking to the cell surface is related to the secondary structures and adjacent amino acid residues of glycosylation sites. Systematic analysis of surface glycoprotein trafficking advances our understanding of the mechanisms underlying protein secretion and surface presentation.

Folding State within a Hysteresis Loop: Hidden Multistability in Nonlinear Physical Systems.

Identifying hidden states in nonlinear physical systems that evade direct experimental detection is important as disturbances and noises can place the system in a hidden state with detrimental consequences. We study a cavity magnonic system whose main physics is photon and magnon Kerr effects. Sweeping a bifurcation parameter in numerical experiments (as would be done in actual experiments) leads to a hysteresis loop with two distinct stable steady states, but analytic calculation gives a third folded steady state "hidden" in the loop, which gives rise to the phenomenon of hidden multistability. We propose an experimentally feasible control method to drive the system into the folded hidden state. We demonstrate, through a ternary cavity magnonic system and a gene regulatory network, that such hidden multistability is in fact quite common. Our findings shed light on hidden dynamical states in nonlinear physical systems which are not directly observable but can present challenges and opportunities in applications.

Non-fluorescent transient states of tyrosine as a basis for label-free protein conformation and interaction studies

The amino acids tryptophan, tyrosine, and phenylalanine have been extensively used for different label-free protein studies, based on the intensity, lifetime, wavelength and/or polarization of their emitted fluorescence. Similar to most fluorescent organic molecules, these amino acids can undergo transitions into dark meta-stable states, such as triplet and photo-radical states. On the one hand, these transitions limit the fluorescence signal, but they are also highly environment-sensitive and can offer an additional set of parameters, reflecting interactions, folding states, and immediate environments around the proteins. In this work, by analyzing the average intensity of tyrosine emission under different excitation modulations with the transient state monitoring (TRAST) technique, we explored the photo physics of tyrosine as a basis for such environment-sensitive readouts. From how the dark state transitions of tyrosine varied with excitation intensity and solvent conditions we first established a photophysical model for tyrosine. Next, we studied Calmodulin (containing two tyrosines), and how its conformation is changed upon calcium binding. From these TRAST experiments, performed with 280 nm time-modulated excitation, we show that tyrosine dark state transitions clearly change with the calmodulin conformation, and may thus represent a useful source of information for (label-free) analyses of protein conformations and interactions.

Speaking without vocal folds using a machine-learning-assisted wearable sensing-actuation system

Voice disorders resulting from various pathological vocal fold conditions or postoperative recovery of laryngeal cancer surgeries, are common causes of dysphonia. Here, we present a self-powered wearable sensing-actuation system based on soft magnetoelasticity that enables assisted speaking without relying on the vocal folds. It holds a lightweighted mass of approximately 7.2 g, skin-alike modulus of 7.83 × 105 Pa, stability against skin perspiration, and a maximum stretchability of 164%. The wearable sensing component can effectively capture extrinsic laryngeal muscle movement and convert them into high-fidelity and analyzable electrical signals, which can be translated into speech signals with the assistance of machine learning algorithms with an accuracy of 94.68%. Then, with the wearable actuation component, the speech could be expressed as voice signals while circumventing vocal fold vibration. We expect this approach could facilitate the restoration of normal voice function and significantly enhance the quality of life for patients with dysfunctional vocal folds.

Graphene Oxide Wrapped VO2 Nanobelts for Calendar‐Life Zn Storage Devices

AbstractAqueous zinc ion batteries (AZIBs) are thought to be emerging energy storage systems due to their features with high safety, low cost, and eco‐friendliness. They possess potential applications in smart grids and wearable devices. However, it is still a challenge to design suitable cathode materials that matches well with anode. Herein, graphene oxide (GO) coated VO2 nanobelts are prepared through a facile hydrothermal route. The Zn//VO2@GO batteries deliver a specific capacity of 323 mA h g−1 at a current density of 0.1 A g−1. It maintains an 88% of capacity retention rate at 5 A g−1 after 1000 times cycling. Moreover, the assembled flexible cells demonstrate excellent mechanical stability under different folding conditions.