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Results for “interfacial resistance”

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3 recordsLinked to original sources
PubMed2026

Direct Modeling of the Interfacial Resistance in All-Solid-State Battery.

Interfacial reconstruction and its associated high resistance govern the performance of all-solid-state batteries (ASSBs). However, indirectly inferring interfacial potentials from bulk band alignments masks the true solid-solid electrochemistry, causing orders-of-magnitude discrepancies in predicting space-charge layer (SCL) resistances and impeding interface screening. Herein, by traversing 310 distinct interfaces from &#x223c;29,000 literatures, we develop a non-empirical numerical procedure that directly maps lithium&#x2011;ion redistribution to interfacial resistance by integrating ligand&#x2011;field theory with the SCL model. Considering electric potential differences and intrinsic carrier properties during interfacial reconstruction via a modified ligand-field splitting strength (MLFSS) descriptor yields unprecedented bridging between modeling and measurement, reducing predicted resistance discrepancies from over ten orders of magnitude to within two. On this basis, we resolve the highly system-dependent controversy over oxide interfacial resistances by identifying extreme MLFSS disparities (>3.5&#xa0;eV) as the decisive factor, while emphasizing ion&#x2011;intercalation sulfides (<0.2&#xa0;eV) as cathodes for their intrinsic SCL suppression. The predictive capability of this tunable criterion is validated in an all-sulfide V0.5Cr1.5S4/Li10GeP2S12/75% Li2S-24% P2S5-1% P2O5/Li prototype. The resulting ultralow interfacial resistance of 8.8 &#x3a9; cm2 ensures superior cycling stability at an active-material energy density of 562&#xa0;Wh kg-1, establishing a practical paradigm for breaking the energy and kinetics trade-off in ASSBs.

all&#x2010;solid&#x2010;state battery↗
PubMed2024

Micro-interfacial behavior of antibiotic-resistant bacteria and antibiotic resistance genes in the soil environment: A review.

Overutilization and misuse of antibiotics in recent decades markedly intensified the rapid proliferation and diffusion of antibiotic resistance genes (ARGs) within the environment, thereby elevating ARGs to the status of a global public health crisis. Recognizing that soil acts as a critical reservoir for ARGs, environmental researchers have made great progress in exploring the sources, distribution, and spread of ARGs in soil. However, the microscopic state and micro-interfacial behavior of ARGs in soil remains inadequately understood. In this study, we reviewed the micro-interfacial behaviors of antibiotic-resistant bacteria (ARB) in soil and porous media, predominantly including migration-deposition, adsorption, and biofilm formation. Meanwhile, adsorption, proliferation, and degradation were identified as the primary micro-interfacial behaviors of ARGs in the soil, with component of soil serving as significant determinant. Our work contributes to the further comprehension of the microstates and processes of ARB and ARGs in the soil environments and offers a theoretical foundation for managing and mitigating the risks associated with ARG contamination.

Soil Microbiology↗
PubMed2026

Genomic and structural insights into the atpB L173I substitution: modulation of the F&#x2080; rotor architecture in Mycobacterium tuberculosis ATP synthase and altered Bedaquiline binding dynamics.

The F&#x2080;F&#x2081; ATP synthase of Mycobacterium tuberculosis (M. tuberculosis) is an essential membrane-embedded rotary motor responsible for ATP synthesis and maintenance of the proton motive force in bacteria. The transmembrane F&#x2080; domain comprises the c-subunit (atpE) and the a-subunit (atpB). Their coordinated interactions are needed for proton translocation and torque generation. Bedaquiline (BDQ), FDA-approved diarylquinoline for the treatment of multidrug-resistant tuberculosis (MDR-TB), targets the F&#x2080; motor by binding at the a-c interface and inhibiting rotary catalysis. To the best of our knowledge, this study represents the first attempt to analyze the effects of mutations in the atpB protein on its structural stability in the F&#x2080; domain, thereby highlighting the novelty of this work. In this study, we integrated Indian whole-genome sequencing (WGS) datasets (PRJNA37907) with long-timescale (1000 ns) membrane-embedded molecular dynamics (MD) simulations. Among 57 atpB mutations identified from WGS analysis, L173I was selected for structural and MD analysis. L173I is located at the atpB-atpE interface near the BDQ-binding region, despite V177L and S184A showing higher prevalence. Comparative MD simulations encompassed four systems: wild-type apo, wild-type with BDQ, L173I apo, and L173I with BDQ. Structural interrogation revealed that the L173I substitution induces subtle destabilization of the global fold of the atpB-atpE complex relative to the apo state, while more critically attenuating inter-subunit contacts between the a-subunit and the c-ring. These perturbations provide a mechanistic rationale for reduced BDQ susceptibility, arising from altered interfacial dynamics rather than complete abrogation of drug binding. This integrative genomic-structural framework advances our understanding of ATP synthase-mediated resistance in M. tuberculosis.

Diarylquinolines↗