In this work, considering anisotropic and homogeneous Bianchi type-V universe we investigated Kaniadakis holographic dark energy (KHDE). It is demonstrated that the equation of state (EoS) parameter has a transition from the quintessence era to the phantom era for the chosen model. Additionally, in the late time of the universe, EoS parameter behaves like a cosmological constant ([Formula: see text]) with an IR (Infrared) cut-off apparent horizon in case of a particular form of deceleration parameter. We reconstructed correspondence between the KHDE and tachyon, quintessence and k-essence scalar fields. Also, our numerical solutions have been shown in graphs for EoS parameter and scalar fields.

Background Human serum albumin (HSA) is often selected as a subject of any study because albumin is the most abundant protein in human blood plasma. NMR is recognized as a valuable method to determine the structure of proteins-ligand and protein-drug complexes. Objective – Aim of the study In this study, protein drug interactions were investigated using 5-Fluorouracil anti-cancer drug and human serum albumin protein. Materials and methods In this context 400 MHz NMR spectrometry was used and NMR relaxation rates in drug-albumin complex were investigated with respect to increase albumin concentration and increase in 5-Fluorouracil (5-FU)-albumin solution temperature. Results The results of this study indicated that 5-FU had a weak association with albumin, and it easily dissociated from the protein to which it was attached. Conclusion The obtained results also gave us useful information about molecular dynamics of drug-albumin interactions.

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The development of modern spectroscopic methods has facilitated and accelerated structure analysis. The NMR method is the most popular way to perform structural analysis of compounds with very complex structures.D2O is a solvent that is frequently used in NMR analysis of both chemical molecules and many biological molecules such as drugs, proteins, and enzymes. In this paper, the study of residual water in proton drug-added protein solutions was carried out via NMR relaxation. The spin-lattice (T1) and the spin-spin relaxation (T2) times of residual water in drug-added protein solutions were studied depending on temperature by Avance Bruker 400 MHz 1H-NMR Spectrometer, and activation energies (Ea) and rotational correlation times (τ0 and τc) have been determined for T1 and T2 relaxation times.