Influence of Molecular Weight and Lithium Bis(trifluoromethanesulfonyl)imide on the Thermal Processability of Poly(ethylene oxide) for Solid-State Electrolytes.

New energy systems such as all-solid-state battery (ASSB) technology are becoming increasingly important today. Recently, researchers have been investigating the transition from the lab-scale production of ASSB components to a larger scale. Poly(ethylene oxide) (PEO) is a promising candidate for the large-scale production of polymer-based solid electrolytes (SPEs) because it offers many processing options. Hence, in this work, the thermal processing route for a PEO-Lithium bis(trifluoromethylsulfonyl)imide (LiTFSI) SPE in the ratio of 20:1 (EO:Li) is investigated using kneading experiments. Here, we clearly show the sensitivity of PEO during thermal processing, especially for high-molecular-weight PEO (Mw = 600,000 g mol-1). LiTFSI acts as a plasticizer for low-molecular-weight PEO (Mw = 100,000 g mol-1), while it amplifies the degradation of high-molecular-weight PEO. Further, LiTFSI affects the thermal properties of PEO and its crystallinity. This leads to a higher chain mobility in the polymer matrix, which improves the flowability. In addition, the spherulite size of the produced PEO electrolytes differs from the molecular weight. This work demonstrates that low-molecular-weight PEO is more suitable for thermal processing as a solid electrolyte due to the process stability. High-molecular-weight PEO, especially, is strongly influenced by the process settings and LiTFSI.

Glycolytic flux control by drugging phosphoglycolate phosphatase.

Targeting the intrinsic metabolism of immune or tumor cells is a therapeutic strategy in autoimmunity, chronic inflammation or cancer. Metabolite repair enzymes may represent an alternative target class for selective metabolic inhibition, but pharmacological tools to test this concept are needed. Here, we demonstrate that phosphoglycolate phosphatase (PGP), a prototypical metabolite repair enzyme in glycolysis, is a pharmacologically actionable target. Using a combination of small molecule screening, protein crystallography, molecular dynamics simulations and NMR metabolomics, we discover and analyze a compound (CP1) that inhibits PGP with high selectivity and submicromolar potency. CP1 locks the phosphatase in a catalytically inactive conformation, dampens glycolytic flux, and phenocopies effects of cellular PGP-deficiency. This study provides key insights into effective and precise PGP targeting, at the same time validating an allosteric approach to control glycolysis that could advance discoveries of innovative therapeutic candidates.