ABSTRACT
This paper delves into an investigation of the solubility characteristics of L-tryptophan within binary solvent systems containing aqueous acetonitrile. The primary emphasis of the study revolves around assessments based on mole fractions. The study utilizes these solubility values to assess thermodynamic constraints, including solution entropies and solution transfer free energetics. The calculated thermodynamic energies are correlated with interaction parameters, including Gibbs free energies and entropies, pertaining to the transfer of L-tryptophanfrom water to binary solvent blends of acetonitrile and water. Mathematical expressions are utilized to determine the transfer Gibbs free energies for chemical interactions, and the consequent entropies are clarified within the framework of solvent-solvent interactions. To expound upon the stability of L-tryptophan within the water-acetonitrile mixed system, we investigate the energetic aspects related to the transfer of chemicals Gibbs free energies. Additionally, standard temperature (298.15 K) is employed to calculate various related physicochemical parameters of solute/solvent.
Subject(s)
Tryptophan , Water , Temperature , Solubility , Thermodynamics , SolventsABSTRACT
Molecular rotor dye thioflavin T (ThT) is almost nonfluorescent in low-viscosity solvents but highly fluorescent when bound to amyloid fibrils. This unique property arises from the rotation of the dimethylaniline moiety relative to the benzothiazole moiety in the excited state, which drives the dye from an emissive locally excited state to a twisted intramolecular charge-transfer state. This process is viscosity-controlled, and therefore, we can use the quantum yield of ThT to assess the viscosity of the environment. In this study, we have investigated the quantum yield of ThT (φThT) in various compositions of six alcoholic solvent mixtures of glycerol with methanol, ethanol, n-propanol, iso-propanol, n-butanol, and tert-butanol. We have proposed an empirical model using φThT as a function of the mole fraction of glycerol to estimate the interaction parameters between the components of the solvent mixtures. This analysis allowed us to predict the extent of nonideality of the solvent mixtures. The Förster-Hoffmann- and Loutfy-Arnold-type power law relationship was established between the quantum yield of ThT and bulk viscosity for solvent mixtures of methanol, ethanol, n-butanol, and tert-butanol with glycerol, and it was found to be similar in nature in all the four mixtures. Applying this knowledge, we proposed a methodology to quantify and predict the bulk viscosity coefficient values of several compositions of n-propanol-glycerol and iso-propanol-glycerol mixtures which have not been previously documented.
ABSTRACT
Interaction between bovine serum albumin (BSA) and phosphorus heterocycles (PHs) was studied using multi-spectroscopic techniques. The results indicated the high binding affinity of PHs to BSA as it quenches the intrinsic fluorescence of BSA. The experimental data suggested the fluorescence quenching mechanism between PHs and BSA as a dynamic quenching. From the UV-vis studies, the apparent association constant (Kapp) was found to be 9.25×102, 1.27×104 and 9.01×102 L/mol for the interaction of BSA with PH-1, PH-2 and PH-3 respectively. According to the Förster's non-radiation energy transfer (FRET) theory, the binding distances between BSA and PHs were calculated. The binding distances (r) of PH-1, PH-2 and PH-3 were found to be 2.86, 3.03, and 5.12 nm, respectively, indicating energy transfer occurs between BSA and PHs. The binding constants of the PHs obtained from the fluorescence quenching data were found to be decreased with increase of temperature. The negative values of the thermodynamic parameters ΔH, ΔS and ΔG at different temperatures revealed that the binding process is spontaneous; hydrogen bonds and van der Waals interaction were the main force to stabilize the complex. The microenvironment of the protein-binding site was studied by synchronous fluorescence and circular dichroism (CD) techniques and data indicated that the conformation of BSA changed in the presence of PHs. Finally, we studied the BSA-PHs docking using Autodock and results suggest that PHs is located in the cleft between the domains of BSA.
ABSTRACT
Reaction of o-azidobenzenesulfonamides with ethyl carbonochloridate afforded the corresponding amide derivatives, which gave 3-ethoxy-1,2,4-benzothiadiazine 1,1-dioxides through an intramolecular aza-Wittig reaction. The reaction was found to be general through the synthesis of a number of benzothiadiazine 1,1-dioxides. Acid-catalyzed hydrolysis of 3-ethoxy-1,2,4-benzothiadiazine 1,1-dioxides furnished the 2-substituted benzothiadiazine-3-one 1,1-dioxides in good yields and high purity, which is the core moiety of RSV inhibitors.
