Sorbents for treatment of hereditary hemochromatosis

Synergistic Aqueous Biphasic Separation of No‐Carrier‐Added 71,72As from a Gallium Oxide Target Using Green Tea Polyphenols

“…Ga 3 + having a closed electron shell, displays redox inertia and can compete for the Fe 3 + position in biomolecules. [31] Catechin forms 1 : 1 Fe 3 + : catechin complexes at low pH, 1 : 2 at low to neutral pH, and 1 : 3 at neutral to high pH [32] so it can be said that gallium mimics iron in this system and is preferentially extracted in PEG + Catechin rich phase. Toreggiani et al [33] reported that catechin acted like a bidentate ligand when treated with Cu 2 + and Zn 2 + .…”

Studying Peptide-Metal Ion Complex Structures by Solution-State NMR

“…For example, Wilsons disease, that results in a buildup of copper in the body [17] can be treated by copper-chelation therapy [18]; whereas copper deficiency due to Menkes disease [19], which causes copper deficiency in cells, is usually fatal, although copper therapy has been shown to ameliorate the condition [20]. Likewise an excess of iron, as in that caused by the genetic hemochromatosis [21], is treated using iron-binding sorbents [22]; and iron deficiency, anemia, is treated by iron supplements or transfusion [23].…”

“…Destabilization and misfolding caused by manganese-binding in prion disease [149] was studied with a 30-amino acid peptide comprising three repeats of a decapeptide repeat in the C-terminal region of the calcium protein, Cap43, that was probed using 1D 1 H-NMR to follow line-broadening upon binding and elucidate the role of divalent ions in the pathogenesis of prion disease [150]. Mn(II) ion binding to a peptide derived from amyloid beta, Aβ (13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23), was also studied by measuring line-broadening upon binding by 1D 1 H-NMR [151].…”

“…A model of the structure of a complex of Co(II) and a fragment of amyloid beta protein, Aβ (13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23), was determined by canonical methodology on a sample with a 1:0.01 molar ratio of peptide-to-cobalt. The intensity of the signals were measured as a function of titration and signals with reduced intensity were considered to be proximate to the cobalt ion and served as the cobalt binding center [151].…”