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Two different synchronous spectrofluorimetric approaches for simultaneous determination of febuxostat and ibuprofen.

ABSTRACT: Two green, simple and sensitive synchronous spectrofluorimetric methods were developed for the first time for the simultaneous estimation of febuxostat (FEB) and ibuprofen (IBU). Method I is constant-wavelength synchronous spectrofluorimetry where FEB and IBU were recorded at 329 and 258 nm, respectively, using Δλ of 40 nm. Method II is constant-energy synchronous spectrofluorimetry using a wavenumber interval of -4000 cm^-1. All measurements were carried out in a borate buffer of pH 7 and distilled water for dilution which increased the methods' greenness. The two methods were rectilinear over concentration ranges of 30.0-700.0 ng ml^-1 and 0.5-9.0 µg ml^-1 in the first method and 20.0-500.0 ng ml^-1 and 0.1-8.0 µg ml^-1 in the second method for FEB and IBU, respectively. High sensitivity was attained for the two drugs with limits of quantitations (LODs) down to 0.41 and 5.51 ng ml^-1 in the first method and 0.25 and 3.32 ng ml^-1 in the second method for FEB and IBU, respectively. Recovery percentages were in the range of 97.3-101.9% after extraction from spiked human plasma samples, demonstrating high bioanalytical applicability. The two methods were further applied to tablet dosage forms with good recovery results. The methods' greenness was assessed according to the analytical Eco-Scale and Green Analytical Procedure Index guidelines.

SUBMITTER: Magdy G

PROVIDER: S-EPMC8150019 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:The investigation of the mechanism of protein folding is complicated by the context dependence of the rates of intramolecular contact formation. Methods based on site-specific labeling and ultrafast spectroscopic detection of fluorescence signals were developed for monitoring the rates of individual subdomain folding transitions in situ, in the context of the whole molecule. However, each site-specific labeling modification might affect rates of folding of near-neighbor structural elements, and thus limit the ability to resolve fine differences in rates of folding of these elements. Therefore, it is highly desirable to be able to study the rates of folding of two or more neighboring subdomain structures using a single mutant to facilitate resolution of the order and interdependence of such steps. Here, we report the development of the "Transfer-Quench" method for measuring the rate of formation of two structural elements using a single triple-labeled mutant. This method is based on Förster resonance energy transfer combined with fluorescence quenching. We placed the donor and acceptor at the loop ends, and a quencher at an α-helical element involved in the node forming the loop. The folding of the triple-labeled mutant is monitored by the acceptor emission. The formation of nonlocal contact (loop closure) increases the time-dependent acceptor emission, while the closure of the labeled helix turn reduces this emission. The method was applied in a study of the folding mechanism of the common model protein, the B domain of staphylococcal protein A. Only natural amino acids were used as probes, and thus possible structural perturbations were minimized. Tyr and Trp residues served as donor and acceptor at the ends of a long loop between helices I and II, and a Cys residue as a quencher for the acceptor. We found that the closure of the loop (segment 14-33) occurs with the same rate constant as the nucleation of helix HII (segment 33-29), in line with the nucleation-condensation model.

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Two different synchronous spectrofluorimetric approaches for simultaneous determination of febuxostat and ibuprofen.

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