This paper reports the influence of surface charge of the micelles on to the photophysical properties of a cinchonine dication (C2+) fluorophore in anionic, sodium dodecylsulphate (SDS), surfactant at premicellar, micellar and post-micellar concentrations in aqueous phase at room temperature. The magnitude of edge excitation red shift (EERS) in the fluorescence maximum of C2+ in bulk water solution is 1897 cm- 1 whereas, in the case of SDS it is observed to be 1984 cm- 1. The fluorescence decay curve of C2+ fits with multi exponential functions in the micellar system. The increase in lifetime of C2+ in SDS has been attributed to the increase in radiative rate due to the incorporation of C2+ at the micelle -water interface. The value of dynamic quenching constant determined is 16.9 M- 1. The location of the probe molecule in micellar systems has been justified by a variety of spectral parameters such as dielectric constant, ET (30), viscosity, EERS, average fluorescence decay time, radiative and non-radiative rate constants. All experimental results suggest that the C2+ molecule binds strongly with the SDS micelles and resides at micellar-water interface. The binding constant (Kb) calculated (3.85 × 105 M- 1) for C2+ in SDS revealed that the electrostatic forces mediate charge probe-micelle association.

The review provides an overview of recent developments and applications of capillary electromigration (CE) methods for the determination of important physicochemical parameters of various (bio)molecules and (bio)particles. These parameters include actual and limiting (absolute) ionic mobilities, effective electrophoretic mobilities, effective charges, isoelectric points, electrokinetic potentials, hydrodynamic radii, diffusion coefficients, relative molecular masses, acidity (ionization) constants, binding constants and stoichiometry of (bio)molecular complexes, changes of Gibbs free energy, enthalpy and entropy and rate constants of chemical reactions and interactions, retention factors and partition and distribution coefficients. For the determination of these parameters, the following CE methods are employed: zone electrophoresis in a free solution or in sieving media, isotachophoresis, isoelectric focusing, affinity electrophoresis, electrokinetic chromatography, and electrochromatography. In the individual sections, the procedures for the determination of the above parameters by the particular CE methods are described.

UNASSIGNED: Modern drug discovery revolves around designing ligands that target the chosen biomolecule, typically proteins. For this, the evaluation of affinities of putative ligands is crucial. This has given rise to a multitude of dedicated computational and experimental methods that are constantly being developed and improved.
UNASSIGNED: In this review, the authors reassess both the industry mainstays and the newest trends among the methods for protein - small-molecule affinity determination. They discuss both computational affinity predictions and experimental techniques, describing their basic principles, main limitations, and advantages. Together, this serves as initial guide to the currently most popular and cutting-edge ligand-binding assays employed in rational drug design.
UNASSIGNED: The affinity determination methods continue to develop toward miniaturization, high-throughput, and in-cell application. Moreover, the availability of data analysis tools has been constantly increasing. Nevertheless, cross-verification of data using at least two different techniques and careful result interpretation remain of utmost importance.

The review discusses electrochemical methods for analysis of drug interactions with DNA. The electroanalysis method is based on the registration of interaction-induced changes in the electrochemical oxidation potential of heterocyclic nitrogenous bases in the DNA molecule and in the maximum oxidation current amplitude. The mechanisms of DNA-drug interactions can be identified based on the shift in the electrooxidation potential of heterocyclic nitrogenous bases toward more negative (cathodic) or positive (anodic) values. Drug intercalation into DNA shifts the electrochemical oxidation potential to positive values, indicating thermodynamically unfavorable process that hinders oxidation of nitrogenous bases in DNA. The potential shift toward the negative values indicates electrostatic interactions, e.g., drug binding in the DNA minor groove, since this process does not interfere with the electrochemical oxidation of bases. The concentration-dependent decrease in the intensity of electrochemical oxidation of DNA bases allows to quantify the type of interaction and calculate the binding constants.

Drug binding to plasma proteins influences processes such as liberation, adsorption, disposition, metabolism, and elimination of drugs, which are thus one of the key steps of a new drug development. As a result, the characterization of drug-protein interactions is an essential part of these time- and money-consuming processes. It is important to determine not only the binding strength and the stoichiometry of interaction, but also the binding site of a drug on a protein molecule, because two drugs with the same binding site can mutually affect free drug concentration. Capillary electrophoresis-frontal analysis with mobility shift affinity capillary electrophoresis is one of the most used affinity capillary electrophoresis methods for the characterization of these interactions. In this study, a well-known sensitivity problem of most capillary electrophoresis-frontal analyses using ultraviolet detection is solved by its combination with contactless conductivity detection, which provided sixfold lower limits of quantitation and detection. Binding parameters of the human serum albumin-salicylic acid model affinity pair were evaluated by this newly developed approach and by the classical approach with ultraviolet detection primarily used for their mutual comparison. The results of both approaches agreed well and are also in agreement with literature data obtained using different techniques.

The incorporation of phosphorothioate linkages has recently been extensively employed in therapeutic oligonucleotides. For their separation and quality control, new high-efficient and high-sensitive analytical methods are needed. In this work, a new affinity capillary electrophoresis method has been developed and applied for the separation of a potential anticancer drug, 2\',3\'-cyclic diadenosine diphosphorothioate (Rp, Rp) (ADU-S100), and three recently newly synthesized diastereomers of its difluorinated derivative, 3\',3\'-cyclic di(2\'-fluoro, 2\'-deoxyadenosine phosphorothioate). The separation was performed in the various background electrolytes (BGEs) within a pH range 5-9 using several native and derivatized cyclodextrins (CDs) as chiral additives of the BGE. Relatively good separations were obtained with β-, γ-, and 2-hydroxypropyl-γ-CDs in some of the BGEs tested. However, the best separation was achieved using the 2-hydroxypropyl-β-CD chiral selector at 43.5 mM average concentration in the BGE composed of 40 mM Tris, 40 mM tricine, pH 8.1. Under these conditions, all the previous four cyclic dinucleotides (CDNs) were baseline separated within 4 min. Additionally, the average apparent binding constants and the average actual ionic mobilities of the complexes of all four CDNs with 2-hydroxypropyl-β-CD in the above BGE were determined. The formed complexes were found to be relatively weak, with the average apparent binding constants in the range of 12.2-94.1 L mol-1 and with the actual ionic mobilities spanning the interval (-7.8 to -12.7) × 10-9 m2 V-1 s-1. The developed method can be applied for the separation, analysis, and characterization of the above and similar CDNs.

Binding towards human serum albumin (HSA) and α1-acid glycoprotein (AGP) of three approved fibroblast growth factor receptor (FGFR) inhibitors ponatinib (PON), nintedanib (NIN) and erdafitinib (ERD), as well as the experimental drug KP2692 was studied by means of spectrofluorometric and UV-visible spectrophotometric methods. Additionally, proton dissociation processes, lipophilicity, and fluorescence properties of these four molecules were investigated in detail. The FGFR inhibitors were predominantly presented in their single protonated form (HL+) at pH 7.4 (at blood pH). At gastric pH (pH 1-2) the protonated forms (+1 - +3) are present, which provide relatively good aqueous solubility of the drugs. All of the four inhibitors are highly or extremely lipophilic at pH 7.4 (logD7.4 ≥ 2.7). At acidic pH 2.0 PON and ERD are rather lipophilic, NIN is amphiphilic, while KP2692 is highly hydrophilic. All four compounds bind to HSA and AGP. Moderate binding of PON, KP2692 and NIN was found towards albumin (logK\' = 4.5-4.7), while their affinity for AGP was about one order of magnitude higher (logK\' = 5.2-5.7). ERD shows a larger affinity for both proteins (logK\'HSA ≈ 5.2, logK\'AGP ≈ 7.0). The computed constants were used to model the distribution of the FGFR inhibitors in blood plasma under physiological and pathological (acute phase) conditions. The changing levels of the two proteins under pathological conditions compensate each other for PON and NIN, so that the free drug fractions do not change considerably. In the case of ERD the higher AGP levels distinctly reduce the free available fraction of the drug. Comparison with clinical pharmacokinetic data indicates that the here presented solution distribution studies can very well predict the conditions in cancer patients.

The work described is focused on a newly developed colorimetric Schiff base fluorescent sensor that exhibits a \"turn-off\" response when detecting fluoride ions (F-) in an aqueous environment. The confirmation of the recognition event is accomplished through fluorescence titration, absorbance titration, and Density Functional Theory (DFT) calculation study. From the results, it is determined that the detection limit of F- is 2.35 × 10-8 M which is much lower than the World Health Organization (WHO) permissible limit for drinking water while the binding constant was obtained to be 0.1 × 106 M-1 indicating a moderate affinity for the fluoride ions. Furthermore, the binding stoichiometry between the Probe L and F- was found to be 1:1 which is evidenced by the Job\'s plot and DFT calculation study. Overall, the novel sensor\'s impressive sensitivity and selectivity make it a promising candidate for the detection of fluoride ions in aqueous media, particularly for monitoring drinking water quality to ensure compliance with WHO guidelines.

The effect of dimethylsulfoxide (DMSO) and diethylsulfoxide (DESO) on binding between quinine sulfate (QS) and DNA was studied by virtue of UV-Vis absorption, steady-state fluorescence spectroscopies, and fluorescence polarization measurements. The binding constant was determined at three different temperatures and the values of standard Gibbs energy change, enthalpy and entropy of binding were determined. The mechanism of binding and the effect of sulfoxides on this process was revealed. The values of binding constant, fluorescence polarization and iodide quenching studies confirmed that the main binding mode in QS-DNA system is groove binding. Addition of sulfoxides does not change the binding mechanism. Moreover, with addition of sulfoxides binding constant increases due to the removal of water molecules from DNA grooves making them more available for QS molecules. To explain the effect of DMSO and DESO on QS-DNA binding the photophysical properties of QS in aqueous solutions of DMSO and DESO were also studied. On the basis of quantum yield of QS in water, DMSO and DESO the types of intermolecular interactions were discussed. The obtained results show that quantum yield of QS in sulfoxides is lower compared with that in water and aqueous solution of 0.1 M H2SO4. QS forms ground state complexes with both DMSO and DESO that are stronger fluorophores compared with free QS molecules.

Ingenious nanomaterials with improved biocompatibility and multifunctional properties are gaining vital significance in biomedical applications, including advanced drug delivery and nanotheranostics. In a biological system, these nanoparticles interact with serum proteins forming a dynamic corona that affects their biological or toxicological properties producing undesirable effects. Thus, the current study focuses on the synthesis of sulphur-doped zinc oxide nanoparticles (ZnO/S NPs) and characterizing their mechanism of interaction with serum proteins using multispectroscopic approach. ZnO/S NPs were synthesized by employing a co-precipitation approach and characterized using various analytical techniques. The results of interaction studies demonstrated that ZnO/S NPs interact with serum albumins via the static quenching process. Analysis of thermodynamic parameters (ΔG, ΔH and ΔS) revealed that the binding process is spontaneous, exothermic and van der Waals force or hydrogen bonding plays a major role. The interaction of ZnO/S NPs with tyrosine residue in bovine serum albumin was established by synchronous fluorescence spectroscopy. In addition, the results of UV-visible, circular dichroism, Fourier transform infrared, Forster\'s resonance energy transfer theory and dynamic light scattering spectroscopic studies revealed that the ZnO/S NPs interact with albumin by inducing the conformational changes in secondary structure and reducing the α-helix content.