Solid-state electrolytes are the key to the development of lithium-based batteries with dramatically improved energy density and safety. Inspired by ionic channels in biological systems, a novel class of pseudo solid-state electrolytes with biomimetic ionic channels is reported herein. This is achieved by complexing the anions of an electrolyte to the open metal sites of metal-organic frameworks (MOFs), which transforms the MOF scaffolds into ionic-channel analogs with lithium-ion conduction and low activation energy. This work suggests the emergence of a new class of pseudo solid-state lithium-ion conducting electrolytes.

Creating Lithium-Ion Electrolytes with Biomimetic Ionic Channels in Metal–Organic Frameworks

On the difference in cycling behaviors of lithium-ion battery cell between the ethylene carbonate- and propylene carbonate-based electrolytes

https://ir.nctu.edu.tw:443/bitstream/11536/28534/1/000177955400028.pdf

Ionic conductivity enhancement of the plasticized PMMA/LiClO4 polymer nanocomposite electrolyte containing clay

The interactions of metoprolol tartrate (MPT) and guaifenesin (GF) drugs with human serum albumin (HSA) and human hemoglobin (HMG) proteins at pH 7.4 were studied by fluorescence and circular dichroism (CD) spectroscopy. Drugs quenched the fluorescence spectra of HSA and HMG proteins through a static quenching mechanism. For each protein-drug system, the values of Stern-Volmer quenching constant, bimolecular quenching constant, binding constant and number of binding site on the protein molecules were determined at 288.15, 298.15, 310.15 and 318.15 K. It was found that the binding constants of HSA-MPT and HSA-GF systems were smaller than those of HMG-MPT and HMG-GF systems. For both drugs, the affinity of HMG was much higher than that of HSA. An increase in temperature caused a negative effect on the binding reactions. The number of binding site on blood proteins for MPT and GF drugs was approximately one. Thermodynamic parameters showed that MPT interacted with HSA through electrostatic attraction forces. However, hydrogen bonds and van der Waals forces were the main interaction forces in the formation of HSA-GF, HMG-MPT and HMG-GF complexes. The binding processes between protein and drug molecules were exothermic and spontaneous owing to negative ∆H and ∆G values, respectively. The values of binding distance between protein and drug molecules were calculated from Forster resonance energy transfer theory. It was found from CD analysis that the bindings of MPT and GF drugs to HSA and HMG proteins altered the secondary structure of HSA and HMG proteins.

Characterization of the Binding of Metoprolol Tartrate and Guaifenesin Drugs to Human Serum Albumin and Human Hemoglobin Proteins by Fluorescence and Circular Dichroism Spectroscopy

The interactions of tramadol hydrochloride (THC) and 5-azacytidine (AZA) drugs with human serum albumin (HSA) and human hemoglobin (HMG) proteins were investigated by fluorescence, UV absorption and circular dichroism (CD) spectroscopy at pH 7.4 and different temperatures. The UV absorption spectra and the fluorescence quenching of HSA and HMG proteins indicated the formation of HSA–THC and HMG–THC complexes via static quenching mechanism. AZA did not interact with HSA and HMG proteins. It was found that the formation of HMG–THC complex was stronger than that of HSA–THC complex. The stability of HSA–THC and HMG–THC complexes decreased with increasing temperature. The number of binding site was found as one for HSA–THC and HMG–THC systems. Negative enthalpy change (Δ H ) and Gibbs free energy change (Δ G ) and positive entropy change (Δ S ) values were obtained for these systems. The binding of THC–HSA and HMG proteins was spontaneous and exothermic. In addition, electrostatic interactions between protein and drug molecules played an important role in the binding processes. The results of CD analysis revealed that the addition of THC led to a significant conformational change in the secondary structure of HSA protein, on the contrary to HMG protein.

Spectroscopic investigations of the interactions of tramadol hydrochloride and 5-azacytidine drugs with human serum albumin and human hemoglobin proteins

Vibrational spectroscopic studies on ion solvation of lithium perchlorate in propylene carbonate + N,N-dimethylformamide mixtures.

Characterization of the interaction between 8-bromoadenosine with human serum albumin and its analytical application.

This work was designed to study the interaction between 5-Methyluridine and human serum albumin (HSA) under simulative physiological conditions using fluorescence spectroscopy in combination with molecular modeling technique for the first time. Static quenching was suggested by the fluorescence measurement. The binding constants (K) were calculated according to the relevant fluorescence data at different conditions including temperature. Thermodynamic parameter, different conditions including temperature to determine enthalpy change and entropy change, indicating the hydrophobic force played a major role in the binding interaction between 5-Methyluridine and HSA. The experimental result was in correspondence with molecular modeling theory.

A study on the interaction between 5-Methyluridine and human serum albumin using fluorescence quenching method and molecular modeling

The infrared (IR) and Raman spectra of propylene carbonate (PC) containing various concentrations of LiClO4 have been measured and analyzed. The difference in spectra of PC with and without LiClO4 was attributed to the interaction of the PC molecules and lithium ions. This interaction occurs mainly on the carbonyl oxygen atom of the PC molecule. The ring deformation, symmetric ring deformation, carbonyl stretching and stretching of ring oxygens for PC are sensitive to this interaction. The solvation number of Li+ is also calculated. On the other hand, the structure of the ClO− 4 is also affected by PC molecule, forming the solvent separated ion pairs.

A Vibrational Spectroscopic Study of Ion Solvation in Lithium Perchlorate/Propylene Carbonate Electrolyte

This study was designed to investigate the interaction between (S)-2-(9H-purin-6-ylamino)-4-(methylthio) butanoic acid (PYMBA) and human serum albumin (HSA) using fluorescence spectroscopy The combination of UV absorption and molecular docking under simulative physiological conditions was also applied to comprehensively understand the binding mechanism of PYMBA to HSA Fluorescence data indicated that PYMBA has a strong ability to quench the intrinsic fluorescence of HSA The binding constants (K) at different temperatures, thermodynamic parameters including enthalpy change (DeltaH) and entropy change (DeltaS) of PYMBA-HSA were correlated to the relevant fluorescence data, which suggested that the hydrophobic force played a very important role for the PYMBA binding to the HSA The experimental results were in agreement with the results obtained via a molecular docking study The effects of other ions on the binding constants were also studied

Guirong Qu

Papers

Vibrational spectroscopic studies on ion solvation of lithium perchlorate in propylene carbonate + N,N-dimethylformamide mixtures.

Characterization of the interaction between 8-bromoadenosine with human serum albumin and its analytical application.

A study on the interaction between 5-Methyluridine and human serum albumin using fluorescence quenching method and molecular modeling

A Vibrational Spectroscopic Study of Ion Solvation in Lithium Perchlorate/Propylene Carbonate Electrolyte

Interaction of 2-(9H-purin-6-ylamino)-4-(methylthio) butanoic acid with human serum albumin: fluorescence and modeling studies.