Magnesium gluconate is a classical organometallic pharmaceutical compound used for the prevention and treatment of hypomagnesemia as a source of magnesium ion. The present research described the in-depth study on solid state properties viz. physicochemical and thermal properties of magnesium gluconate using sophisticated analytical techniques like PXRD, PSA, FT-IR, UV–Vis spectroscopy, TGA/DTG, and DSC. Magnesium gluconate was found to be crystalline in nature along with the crystallite size ranging from 14.10 to 47.35 nm. The particle size distribution was at d(0.1)=6.552 µm, d(0.5)=38.299 µm, d(0.9)=173.712 µm and D(4,3)=67.122 µm along with the specific surface area of 0.372 m2/g. The wavelength for the maximum absorbance was at 198.0 nm. Magnesium gluconate exhibited 88.51% weight loss with three stages of thermal degradation process up to 895.18 °C from room temperature. The TGA/DTG thermograms of the analyte indicated that magnesium gluconate was thermally stable up to around 165 °C. Consequently, the melting temperature of magnesium gluconate was found to be 169.90 °C along with the enthalpy of fusion of 308.7 J/g. Thus, the authors conclude that the achieved results from this study are very useful in pharmaceutical and nutraceutical industries for the identification, characterization and qualitative analysis of magnesium gluconate for preformulation studies and also for developing magnesium gluconate based novel formulation.
The cardiac Na þ /Ca 2þ exchanger (NCX1.1) serves as the primary means of Ca 2þ extrusion from cardiomyocytes following the rise in intracellular Ca 2þ during contraction. The exchanger is regulated by binding of Ca 2þ to the intracellular domain. This domain is composed of an a-catenin-like domain (CLD) that connects two structurally homologous Ca 2þ binding domains (CBD1 and CBD2) to the transmembrane domain of the exchanger. NMR and X-ray crystallographic studies have provided structures for the isolated CBD1 and CBD2 domains and have suggested how Ca 2þ binding alters their structures and motional dynamics. It remains unknown how Ca 2þ binding to the intact Ca 2þ sensor signals the transmembrane domain to regulate exchanger activity. Site directed spin labeling has been employed to address this question. Conventional EPR experiments have shown that residues in the structured b-sandwich regions are insensitive to Ca 2þ binding and that the a-helical region of CBD2 remains intact upon Ca 2þ binding. Double Electron Electron Resonance (DEER) measurements on doubly labeled constructs revealed that CBD1 and CBD2 are not lengthwise antiparallel in close proximity but rather residues in the distal ends that connect to the CLD are greater than 60 Å apart. DEER measurements between inter-domain residues nearer to the apex of the Ca 2þ sensor are in close enough proximity to be measured by DEER and these distances are sensitive to Ca 2þ binding. These inter-domain distances have been employed to construct a working structural model for CBD12. The current studies are in reasonable agreement with SAXS studies by Hilge et al (PNAS 106:14333-8, 2009) and provide new insight into a structural rearrangement of the intact Ca 2þ sensor that may be involved in regulation of Na þ /Ca 2þ exchange.
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