With 1-methyl-2-pyrrolidinone (NMP) as the solvent, the biodegradable gel polymer electrolyte films are prepared based on poly(vinyl alcohol) (PVA), lithium bis(trifluoromethane)sulfonimide (LiTFSI), and 1-ethyl-3 methylimidazoliumbis(trifluoromethylsulfonyl)imide (EMITFSI) by means of solution casting. The films are characterized to evaluate their structural and electrochemical performance. The 60PVA-40LiTFSI + 10 wt.% EMITFSI system exhibits excellent mechanical properties and a high ionic transference number (0.995), indicating primary ionic conduction in the film. In addition, because of the flexibility of polymer chain segments, its relaxation time is as low as 5.30 × 10−7 s. Accordingly, a high ionic conductivity (3.6 × 10−3 S cm−1) and a wide electrochemical stability window (~5 V) are obtained. The electric double-layer capacitor (EDLC) based on this electrolyte system shows a specific capacitance of 101 F g−1 and an energy density of 10.3 W h kg−1, even after 1000 charge-discharge cycles at a current density of 0.4 A g−1 under a charging voltage of 2 V. All these excellent properties imply that the NMP-soluble 60PVA-40LiTFSI + 10 wt.% EMITFSI gel polymer electrolyte could be a promising electrolyte candidate for electrochemical device applications.

Atomic force microscopy (AFM), transmission electron microscopy (TEM), and confocal laser scanning microscopy were used to investigate the effects of a 50 Hz 0.4 mT magnetic field (MF) on the clustering of purified epidermal growth factor receptors (EGFRs) and EGFRs in Chinese hamster lung (CHL) cell membrane. The results demonstrate that exposing purified EGFRs to the MF for 30 min induces receptor clustering. The peak height of apparent clusters increased from 1.42 +/- 0.18 (sham-exposed) to 3.08 +/- 0.38 nm (exposed) while the mean half-width increased from 21.7 +/- 2.2 to 33.0 +/- 4.0 nm. A similar effect was also observed by TEM. Treatment of purified EGFR with PD153035 (PD), an EGFR-specific tyrosine kinase (TK) inhibitor, inhibited the MF-induced EGFR clustering of the purified proteins, an effect also observed for the receptors in cell membrane in the absence of EGF. These results strongly suggest that the 50 Hz 0.4 mT MF interferes with the EGFR signaling pathway, most likely by interacting with the cytoplasmic TK domain.

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