Quantitative Analysis of Acetazolamide in Solid Dosage Forms with 1H-Nmr Spectroscopy

A rapid and specific proton magnetic resonance spectroscopic method was developed for determining acetazolamide in tablets. Maleic acid was used as the internal standard and DMSO-d₆ served as the NMR solvent. the concentration of drug per unit dose was calculated from the integration values for the resonance signals of acetazolamide at 2.14 ppm and maleic acid at 6.20 ppm. the method using commercial products gave comparable results of those obtained by the method of USP XXIII.     

Resonance Rayleigh scattering and resonance nonlinear scattering of the palladium(II)–acetazolamide chelate with eosin Y and their analytical application

A simple, rapid, and convenient method based on ion association for the determination of acetazolamide has been developed. Acetazolamide can react with palladium(II) to form cationic chelate at sodium acetate–acetic acid buffer solution, which can further react with eosin Y to form an ion association complex. As a result, the resonance Rayleigh scattering, second-order scattering, and frequency doubling scattering intensities are enhanced. Analytical wavelengths of resonance Rayleigh scattering, second-order scattering, and frequency doubling scattering located at 298, 558, and 338?nm, and the linearity range are 0.014–2.5, 0.034–2.5, and 0.119–2.4?µg?mL^?1 respectively. In addition, the optimum conditions and the effect of coexisting substances are investigated. Besides, the structure of ion association complex, the reaction mechanism and the reasons for the enhancement of scattering are discussed through infrared spectra, absorption spectra, and quantum chemical calculations.     

A Case Study on the Use of Binding Free Energies to Screen Inhibitors of Human Carbonic Anhydrase II

We present in this article a case study on the thermodynamics of binding to human carbonic anhydrase II (HCA II) by three well-known inhibitors, viz. (a) acetazolamide (AZM) that directly binds to the catalytic Zn(II) ion at the active site, (b) non-zinc binding 6-hydroxy-2-thioxocoumarin (FC5) (c) 2-[(S)-benzylsulfinyl]benzoic acid (3G1). In each case, the crystal structure or its analogue of inhibitor-bound HCA II has been used to perform classical molecular dynamics (MD) simulation in water till . AZM and FC5 are found to undergo repeated binding and unbinding with markedly different dynamics from the partially buried, substrate-binding hydrophobic pocket near the active site. 3G1, on the other hand, is found to remain mostly at its crystallographic binding site occluded from the active site of HCA II. The associated binding free energies ( ) have been computed using the known MM/GBSA method and compared to the available experimental data. Our results show that encounters several issues including limited sampling of multiple binding sites and incorrect prediction of the affinity of the chosen ligands. Possible use of the simulation results in further construction of Markov state models is also discussed.