Electrolyte Engineering Toward High Performance High Nickel (Ni ≥ 80%) Lithium-Ion Batteries.

High nickel (Ni ≥ 80%) lithium-ion batteries (LIBs) with high specific energy are one of the most important technical routes to resolve the growing endurance anxieties. However, because of their extremely aggressive chemistries, high-Ni (Ni ≥ 80%) LIBs suffer from poor cycle life and safety performance, which hinder their large-scale commercial applications. Among varied strategies, electrolyte engineering is very powerful to simultaneously enhance the cycle life and safety of high-Ni (Ni ≥ 80%) LIBs. In this review, the pivotal challenges faced by high-Ni oxide cathodes and conventional LiPF6 -carbonate-based electrolytes are comprehensively summarized. Then, the functional additives design guidelines for LiPF6 -carbonate -based electrolytes and the design principles of high voltage resistance/high safety novel electrolytes are systematically elaborated to resolve these pivotal challenges. Moreover, the proposed thermal runaway mechanisms of high-Ni (Ni ≥ 80%) LIBs are also reviewed to provide useful perspectives for the design of high-safety electrolytes. Finally, the potential research directions of electrolyte engineering toward high-performance high-Ni (Ni ≥ 80%) LIBs are provided. This review will have an important impact on electrolyte innovation as well as the commercial evolution of high-Ni (Ni ≥ 80%) LIBs, and also will be significant to breakthrough the energy density ceiling of LIBs.

A Novel Potassium Salt Regulated Solvation Chemistry Enabling Excellent Li-Anode Protection in Carbonate Electrolytes.

In lithium-metal batteries (LMBs), the compatibility of Li anode and conventional lithium hexafluorophosphate-(LiPF6 ) carbonate electrolyte is poor owing to the severe parasitic reactions. Herein, to resolve this issue, a delicately designed additive of potassium perfluoropinacolatoborate (KFPB) is unprecedentedly synthesized. On the one hand, KFPB additive can regulate the solvation structure of the carbonate electrolyte, promoting the formation of Li+ FPB- and K+ PF6 - ion pairs with lower lowest unoccupied molecular orbital (LUMO) energy levels. On the other hand, FPB- anion possesses strong adsorption ability on Li anode. Thus, anions can preferentially adsorb and decompose on the Li-anode surface to form a conductive and robust solid-electrolyte interphase (SEI) layer. Only with a trace amount of KFPB additive (0.03 m) in the carbonate electrolyte, Li dendrites' growth can be totally suppressed, and Li||Cu and Li||Li half cells exhibit excellent Li-plating/stripping stability upon cycling. Encouragingly, KFPB-assisted carbonate electrolyte enables high areal capacity LiCoO2 ||Li, LiNi0.8 Co0.1 Mn0.1 O2 (NCM811)||Li, and LiNi0.8 Co0.05 Al0.15 O2 (NCA)||Li LMBs with superior cycling stability, showing its excellent universality. This work reveals the importance of designing novel additives to regulate the solvation structure of carbonate electrolytes in improving its interface compatibility with the Li anode.

Lysosomal degradation of retinal glial AQP4 following its internalization induced by acute ocular hypertension.

The membrane-bound water channel aquaporin-4 plays a significant role in the regulation of water movement within the retina. In retinal ischemia-reperfusion injury, changes in the expression and localization of aquaporin-4 have been reported. Previous studies also suggest that the internalization of several membrane-bound proteins, including aquaporin-4, may occur with or without lysosomal degradation. In this study, the internalization of aquaporin-4 was detected in the ischemic rat retina via double immunofluorescence labeling. Specifically, both aquaporin-4 and the mannose-6-phosphate receptor co-localized post-ischemic injury (10, 30 and 60 min). The same results were found during a 12-h reperfusion window (2, 4 and 8 h, respectively) following 60 min of ischemia. Moreover, the co-expression of aquaporin-4 and lysosomal-associated membrane protein-1 was observed at 1-12 h of reperfusion, with co-expression increasing followed by a gradual decrease. These combined findings suggest that AQP4 is internalized in the ischemic-reperfused retina, and the lysosome is involved in degrading the internalized aquaporin-4 during the reperfusion phase. Both the internalization of aquaporin-4 and its lysosomal degradation may serve as valuable therapeutic targets for managing ischemic-reperfused retinal injury.