Browsing by Author "Arvind Kumar Dixit"

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EDM process parameters optimization for Al-TiO2 nano composite
(IGI Global, 2017) Arvind Kumar Dixit; Richa Awasthi
Titanium aluminide reinforced aluminium based metal matrix nano composite was prepared by stir casting route. Experiments were conducted with Cu electrode using L9 orthogonal array based on the Taguchi method. Discharge current (Lv), Pulse on time (Ton) and Flushing pressure (FP) are selected to calculate Metal removal rate (MRR), Tool wear rate (TWR) and Surface roughness (SR) based on Taguchi's parameter design. Moreover, the signal-to-noise ratios associated with the observed values in the experiments were determined using MINITAB software for MRR, TWR and SR. PCR - TOPSIS method is used to optimize Taguchi's multi response. Optimum parameter setting is found at Discharge current (Lv) 10 A, Pulse on time (Ton) 150 μs and Flushing pressure (FP) 1 kg/cm2. © 2017, IGI Global. All rights reserved.
Insight into the interaction of benzothiazole tethered triazole analogues with human serum albumin: Spectroscopy and molecular docking approaches
(John Wiley and Sons Ltd, 2019) Priyanka Yadav; Jitendra Kumar Yadav; Arvind Kumar Dixit; Alka Agarwal; Satish Kumar Awasthi
The interaction of four benzothiazole tethered triazole analogues (MS43, MS70, MS71, and MS78) with human serum albumin (HSA) was investigated using various spectroscopic techniques (ultraviolet–visible (UV–vis) light absorption, fluorescence, circular dichroism (CD), molecular docking and density functional theory (DFT) studies). Fluorescence quenching constants (~1012) revealed a static mode of quenching and binding constants (Kb ~104) indicating the strong affinity of these analogues for HSA. Further alteration in the secondary structure of HSA in the presence of these analogues was also confirmed by far UV–CD spectroscopy. The intensity loss in CD studied at 222 nm indicated an increase in random coil/β-sheet conformations in the protein. Binding energy values (MS71 (−9.3 kcal mol−1), MS78 (−8.02 kcal mol−1), MS70 (−7.16 kcal mol−1) and MS43 (−6.81 kcal mol−1)) obtained from molecular docking revealed binding of these analogues with HSA. Molecular docking and DFT studies validated the experimental results, as these four analogues bind with HSA at site II through hydrogen bonding and hydrophobic interactions. © 2019 John Wiley & Sons, Ltd.