Thin Li1.3Al0.3Ti1.7(PO4)3-based composite solid electrolyte with a reinforced interface of in situ formed poly(1,3-dioxolane) for lithium metal batteries.

Composite solid electrolytes (CSEs) exhibit great potential due to their advantages of both sufficient strength and high ionic conductivity. However, their interfacial impendence and thickness hinder potential applications. Herein, a thin CSE with good interface performance is designed through the combination of immersion precipitation and in situ polymerization. By employing a nonsolvent in immersion precipitation, a porous poly(vinylidene fluoride-cohexafluoropropylene) (PVDF-HFP) membrane could be rapidly created. The pores in the membrane could accommodate sufficient well-dispersed inorganic Li1.3Al0.3Ti1.7(PO4)3 (LATP) particles. Subsequent in situ polymerized 1,3­dioxolane (PDOL) further protects LATP from reacting with lithium metal and supplies superior interfacial performance. The CSE has a thickness of âˆ¼ 60 µm, ionic conductivity of 1.57 × 10-4 S cm-1, and oxidation stability of 5.3 V. The Li/1.25LATP-CSE/Li symmetric cell has a long cycling performance of 780 h at 0.3 mA cm-2 for 0.3 mAh cm-2. The Li/1.25LATP-CSE/LiFePO4 cell exhibits a discharge capacity of 144.6 mAh/g at 1C and a capacity retention of 97.72 % after 300 cycles. Continuous depletion of lithium salts due to the reconstruction of the solid electrolyte interface (SEI) may be responsible for battery failure. The combination of the fabrication method and failure mechanism gives new insight into designing CSEs.

Interaction mechanism of Cu+/Cu2+ on bovine serum albumin: Vitro simulation experiments by spectroscopic methods.

Copper (Cu) is an essential trace element for organisms, while excessive concentration of Cu is toxic. In order to assess the toxicity risk of copper in different valences, FTIR, fluorescence, and UV-vis absorption techniques were conducted to study the interactions between either Cu+ or Cu2+ and bovine serum albumin (BSA) under vitro simulated physiological condition. The spectroscopic analysis demonstrated that the intrinsic fluorescence emitted by BSA could be quenched by Cu+/Cu2+ via static quenching with binding sites 0.88 and 1.12 for Cu+ and Cu2+, respectively. On the other hand, the constants of Cu+ and Cu2+ are 1.14 × 103 L/mol and 2.08 × 104 L/mol respectively. ΔH is negative whereas ΔS is positive, showing that the interaction between BSA and Cu+/Cu2+ was mainly driven by electrostatic force. In accordance with Föster's energy transfer theory, the binding distance r showed that the transition of energy from BSA to Cu+/Cu2+ is highly likely to happen. BSA conformation analyses indicated that the interactions between Cu+/Cu2+ and BSA could alter the secondary structure of proteins. Current study provides more information of the interaction between Cu+/Cu2+ and BSA, and reveals the potential toxicological effect of different speciation of copper at molecular level.

Comparison of the Effects on Bovine Serum Albumin Induced by Different Forms of Vanadium.

Various forms of vanadium coexist in vivo, and the behavior mechanism is different. An investigation of the separate and simultaneous binding of three vanadium forms with bovine serum albumin (BSA) was performed. VO(acac)2/NaVO3/VOSO4 bound to site I of BSA, and their binding constants were 4.26 × 105, 9.18 × 103, and 4.31 × 102 L mol-1 at 298 K, respectively. VO(acac)2 had the strongest binding ability to BSA and had the most influence on the secondary structure of BSA and the microenvironment of around amino acid residues. The effect of NaVO3 and VOSO4 coexistence on the binding of VO(acac)2 to BSA was therefore further investigated. Both NaVO3 and VOSO4 had an effect on the binding of VO(acac)2 and BSA, with NaVO3 having the most noticeable effect. NaVO3 interfered with the binding process of VO(acac)2 and BSA, increased the binding constant, and changed the binding forces between them. Competition and allosteric effect may be responsible for the change of binding process between VO(acac)2 and BSA in the presence of NaVO3/VOSO4.

A mutispectroscopic study on the structure-affinity relationship of the interactions of bisphenol analogues with bovine serum albumin.

Bisphenol A (BPA) is a recognized endocrine-disrupting chemical (EDC), and its analogues also exert negative effects on health. The structure-affinity relationship between the structures of nine bisphenol (BP) analogues and the conformational changes of bovine serum albumin (BSA) was studied by various characterization methods and molecular docking. BPs including BPA and its analogues, bisphenol B (BPB), bisphenol C (BPC), bisphenol AP (BPAP), bisphenol M (BPM), bisphenol P (BPP), bisphenol Z (BPZ), diethylstilbestrol (DES) and dienestrol (DS) interacted with BSA. At the concentration of 3.85 × 10-5 mol l-1, DS was found to lead to 64% quenching, while BPAP, BPM and DES quenched 60%, 59% and 55% of BSA fluorescence, respectively. The values of ΔH (-19.31-135.42 kJ mol-1) and ΔS (12.52-495.63 J mol-1 K-1) indicated that hydrophobic interactions and hydrogen bonds played important roles in the binding process. The binding constants of DS (8.87 × 104 l mol-1), DES (3.05 × 104 l mol-1), BPAP (1.52 × 104 l mol-1), BPC (1.16 × 104 l mol-1) and BPM (1.10 × 104 l mol-1) to BSA were greater than that of BPA (1.18 × 103 l mol-1) to BSA, indicating that they may exert more negative effects than BPA. The molecular structure differences of these BPs partly affected their ability to bind to BSA. The binding constants of BPB/BPP to BSA were smaller due to the steric hindrance of ethyl and benzene ring. BPs with conjugated double bond structures (DS and DES) and benzene ring structures (BPM, BPP, BPAP) had a greater influence on the conformation of BSA.

Investigation on the interaction of food colorant Sudan III with bovine serum albumin using spectroscopic and molecular docking methods.

Sudan III is a coloring agent used in chemical industries and food additives. This article uses spectroscopic and molecular docking methods to investigate the interaction of Sudan III with bovine serum albumin (BSA) under a physiological condition. Spectroscopic analysis of the emission quenching revealed that the quenching mechanism of BSA by Sudan III was static. The binding sites and constants of Sudan III-BSA complex were observed to be from 0.72 and 6.41 × 102 L·mol-1 to 0.69 and 5.83 × 102 L·mol-1 at 298 and 310 K, respectively. The enthalpy change (ΔH) and entropy change (ΔS) revealed that van der Waals forces and hydrogen bonds stabilized the Sudan III-BSA complex. Energy transfer from tryptophan to Sudan III occurred by a fluorescence resonance energy transfer mechanism, and the r distance (3.32 nm) had been determined. The results of UV-Vis absorption, synchronous, three-dimensional fluorescence, and circular dichroism spectra showed that Sudan III induced conformational changes of BSA. Molecular docking studies revealed that Sudan III situated within subdomain IIA of BSA. A study on the interaction between Sudan III and BSA was of fundamental importance for providing more information about the potential toxicological effect of chemicals at the molecular level.

Interaction of tebuconazole with bovine serum albumin: determination of the binding mechanism and binding site by spectroscopic methods.

This study investigates the interaction between tebuconazole and bovine serum albumin (BSA) in a physiological buffer (pH = 7.4) using the fluorescence quenching method to obtain the apparent binding constants (K) and number of binding sites (n) in the interaction between tebuconazole and BSA. The results revealed that tebuconazole can quench the intrinsic fluorescence of BSA through a static quenching procedure. It also shows that the thermodynamic parameters of enthalpy change (ΔH) and entropy change (ΔS) are negative, indicating that the interaction of tebuconazole with BSA is mainly driven by van der Waals forces and hydrogen bonds. The process of binding was a spontaneous process in which Gibbs free energy change was negative. The distance of r between the donor (BSA) and acceptor (tebuconazole) was calculated to be 0.68 nm based on Forster's non-radiative energy transfer theory. Analysis of synchronous fluorescence, three-dimensional fluorescence and circular dichroism (CD) spectra demonstrates that tebuconazole can induce conformational changes of BSA.