Yahui Sun

Bio: Yahui Sun is an academic researcher from Henan Normal University. The author has contributed to research in topics: Materials science & Analytical Chemistry (journal). The author has an hindex of 1, co-authored 1 publications receiving 50 citations.

Strain modulation on the spin transport properties of PTB junctions with MoC2 electrodes.

Abstract: Based on MoC2 nanoribbons and poly-(terphenylene-butadiynylene) (PTB) molecules, we designed MoC2-PTB molecular spintronic devices and investigated their spin-dependent electron transport properties by using spin-polarized density functional theory and the non-equilibrium Green's function method. As a typical MXene material, it is found that the magnetic contribution of MoC2 nanoribbons mainly comes from the delocalized 3d electron of edge Mo atoms. Owing to the obvious spin-splitting near the Fermi level of the MoC2 nanoribbon electrode, the spin states can be effectively injected into the central scattering region under an external bias voltage. In addition, we also studied the effects of z-axis strain on the spin transport properties of the PTB molecular device, where the strain was controlled within the range of -9% to 9%. Under a compressed strain, spin current increases obviously, and the spin-filtering efficiency (SFE) decreases slightly. Nevertheless, under a tensile strain, we found that the SFE increases but spin current decreases. Moreover, z-axis strain can induce a negative differential resistance (NDR) effect at a high bias point. This work would expand the potential applications of new two-dimensional (2D) materials in the field of molecular spintronic devices.

Electrochemical properties of layered Na x Ni x/2 Mn 1‐x/2 O 2 (0.5 ≤ × ≤ 1.1) with P3 structure as cathode for sodium‐ion batteries

Abstract: The Na properties of Ni and Mn containing layered oxides of the type Na x Ni x/2Mn1−x/2O2 are explored between Na contents of 0.5≤x≤1.1. Charge balance is maintained by adjusting the Ni/Mn ratio. X-ray diffraction and scanning electron microscopy are used to characterize the structure and morphology. The primary phase for all as-synthesized materials is P3, especially at Na contents below x ≤ 0.8. Samples with a Na content of x ≥ 0.9 lead to the formation of Na and Ni secondary phases. The Na storage properties are studied in half cells with two different voltage windows between 1.5–4.0 V and 2.2–4.5 V (vs Na+/Na). Ni and Mn redox are active between 1.5 and 4.0 V accompanying three voltage plateaus at 3.7, 3.0, and 2.1 V, respectively. An additional high-voltage plateau (>4.0 V) is observed when increasing the cutoff voltage to 4.5 V. The initial Na content has a strong influence on the discharge capacity which ranges from 90 mAh g−1 (x = 1.1) to 210 mAh g−1 (x = 0.6). C-rate tests up to 2C and cycle life over 150 cycles are discussed. Overall, the composition Na0.6Ni0.3Mn0.7O2 shows the most favorable properties with respect to capacity retention, rate capability, and initial Coulomb efficiency.

Biophysical Study on the Interaction between Eperisone Hydrochloride and Human Serum Albumin Using Spectroscopic, Calorimetric, and Molecular Docking Analyses.

Abstract: Eperisone hydrochloride (EH) is widely used as a muscle relaxant for patients with muscular contracture, low back pain, or spasticity. Human serum albumin (HSA) is a highly soluble negatively charged, endogenous and abundant plasma protein ascribed with the ligand binding and transport properties. The current study was undertaken to explore the interaction between EH and the serum transport protein, HSA. Study of the interaction between HSA and EH was carried by UV−vis, fluorescence quenching, circular dichroism (CD), Fourier transform infrared (FTIR) spectroscopy, Forster’s resonance energy transfer, isothermal titration calorimetry and differential scanning calorimetry. Tryptophan fluorescence intensity of HSA was strongly quenched by EH. The binding constants (Kb) were obtained by fluorescence quenching, and results show that the HSA–EH interaction revealed a static mode of quenching with binding constant Kb ≈ 104 reflecting high affinity of EH for HSA. The negative ΔG° value for binding indicated that...

Molecular recognition of bio-active flavonoids quercetin and rutin by bovine hemoglobin: an overview of the binding mechanism, thermodynamics and structural aspects through multi-spectroscopic and molecular dynamics simulation studies.

Abstract: The binding of two bio-active flavonoids, quercetin and rutin, with bovine hemoglobin (BHb) was investigated by multi-spectroscopic and computational (molecular docking and molecular dynamics simulation) studies. The two flavonoids were found to quench the intrinsic fluorescence of BHb through a static quenching mechanism. The binding constants at 288 K were observed to be (14.023 ± 0.73) × 104 M-1 and (7.848 ± 0.20) × 104 M-1, respectively for quercetin and rutin binding with BHb. Both rutin and quercetin were observed to increase the polarity around the Trp residues of BHb as indicated by synchronous and 3D spectral studies. No significant alterations in the secondary structural components of the protein were caused during the binding of the flavonoids as studied by CD and FTIR studies. The negative molar Gibbs free energies indicated the spontaneity of the interaction processes while the binding processes were characterized by a negative enthalpy change (ΔH) and a positive entropy change (ΔS). The possibility of energy transfer from the donor (BHb) to the acceptor molecules (flavonoids) was indicated by the FRET studies. According to the fluorescence studies, the flavonoids interact near to the β2-Trp37 residue of BHb. Excellent correlations with the experimental studies were observed from the molecular docking and molecular dynamics (MD) simulation studies. Further investigations established that these flavonoids are efficient in the inhibition of glucose mediated glycation of BHb.

Interaction of Hydralazine with Human Serum Albumin and Effect of β-Cyclodextrin on Binding: Insights from Spectroscopic and Molecular Docking Techniques

Abstract: Biomolecular interaction of hydralazine with human serum albumin (HSA) was studied by fluorescence, ultravoilet, three-dimensional, synchronous, Fourier transform infrared, lifetime fluorescence, resonance Rayleigh scattering, circular dichroism, and molecular docking techniques. The intrinsic fluorescence of HSA was quenched by a static quenching mechanism. The effect of β-cyclodextrin on binding was studied. Binding constants and number of binding sites were evaluated using the Stern–Volmer equation. Thermodynamic parameters (ΔH°, ΔG°, and ΔS°) indicate the involvement of hydrogen bonding with weak van der Waals forces in the interaction. The average binding distance (r) between the HSA and hydralazine was calculated by Fourier resonance energy transfer theory. Molecular docking study confirms the drug binding sites and interaction of hydralazine with amino acid residues.