Interactions of human serum albumin with meloxicam

Thermodynamic investigations of ligand–protein interactions: Binding of the phenazinium dyes phenosafranin and safranin O with human serum albumin

“…Addition of both the dyes leads to decrease in the protein fluorescence intensity ( figure 6A and B). No significant difference was observed in the quenching pattern on excitation at 280 and 295 nm (data not shown) indicating that only Trp residues in the proteins participated in the quenching [46] and this also supports the idea that domain II may be the one of the possible interaction sites of PSF and SO [44]. These data were further reinforced by site selective binding studies.…”

Development of Meloxicam-Human Serum Albumin Nanoparticles for Nose-to-Brain Delivery via Application of a Quality by Design Approach

“…For the MEL-HSA and MEL-HSA-Tween samples, a rapid initial phase was observed for 60 min, followed by a slowing but rising profile. Compared to pure MEL, about a 5 times higher amount, approximately 20% of MEL, was dissolved from the formations within 4 h. Beside this significant increase, we cannot overlook the fact that in the case of the two HSA formulations, the bounded form of MEL was also dissolved due to its rather high binding affinity to HSA (<99%) [46]. At time point of 240 min, the dissolution of MEL from MEL-HSA-Tween was slightly higher than that from the MEL-HSA formulation, but the difference was still significant (**, p = 0.0077), which might be explained by the solubilizing effect of Tween as a surfactant additive.…”

Complexation of insecticide chlorantraniliprole with human serum albumin: Biophysical aspects

“…Till date, many techniques have been exploited for the protein-ligand binding study, including equilibrium dialysis, ultrafiltration, ultracentrifugation, fluorescence, capillary electrophoresis, surface plasmon resonance, calorimetry, surface tension, chromatography, crystallology, and so on [3,4,[16][17][18][19]. Among them, fluorescence spectroscopy has been confirmed to provide the most comprehensively qualitative and quantitative information on the protein-ligand interactions [20,21].…”

“…In this case, the bimolecular quenching constant is calculated and compared to the maximum value possible for diffusion-limited quenching in water ( $ 10 10 M À 1 s À 1 [29]). There have been several literatures [7,8,18,30,31] reporting that HSA quenching because of specific interaction, and the quenching constant has been several magnitudes larger than the maximum value of diffusion-limited quenching in water.…”