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Farid, Naira A.; Youssef, Nadia F.; Abdellatef, Hisham E.; Sharaf, Yasmine A.
Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy, 05/2023, Letnik: 293Journal Article
Display omitted •Fluorescence quenching process has been introduced for the determination of Mirabegron by quenching tyrosine and L-tryptophan fluorophores.•The developed methods were validated as per ICH guidelines and the obtained results were statistically analyzed.•Stern-Volmer relationship was studied at different temperatures for the quenching mechanism recognition which is static or dynamic.•The double log plots were constructed to evaluate binding sites and binding constants.•Greenness of the proposed methods has been assessed to clarify the extent of environmental safety. Green spectrofluorimetric methods have been adopted for the determination of Mirabegron (MG) in pure drug and pharmaceutical dosage form. The developed methods based on fluorescence quenching of tyrosine and L-tryptophan amino acids fluorophores by the effect of Mirabegron as a quencher. Experimental conditions of the reaction were studied and optimized. The Fluorescence quenching (ΔF) values were proportional to the concentration range of MG 2–20 μg/ml for the tyrosine-MG system in buffered media pH 2 and 1–30 μg/ml for L-tryptophan-MG system pH 6. Good correlation coefficients with low detection limits of 0.163 and 0.234 μg/ml for the two systems respectively. Method validation was applied according to ICH guidelines. The cited methods were successively applied for MG determination in tablet formulation. No statistically significant difference between the results of the cited and the reference methods regarding t and F tests. The proposed spectrofluorimetric methods are simple, rapid, eco-friendly and can contribute to MG’s methodologies in quality control labs. Stern-Volmer relationship, the effect of temperature, quenching constant (Kq), and UV spectra were studied to identify the mechanism by which the quenching might occur. The results demonstrated that fluorescence quenching of tyrosine was a dynamic quenching process and L-tryptophan was static. The double log plots were constructed to determine the binding constants and binding sites. The greenness profile of the developed methods has been assessed by Green Analytical procedure index (GAPI) and Analytical Greenness Metric Approach (AGREE).
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