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• W2068675344 abstract "Four new hexadendate chelators, three hydroxyquinoline-based, Csox, O-Trensox, Cox750, and one catecholate-based CacCam-which have comparable skeletal structures and pFe, but widely different partition coefficients, (Kpart), 0.01, 0.02, 1 and 3.2 respectively, have been tested for their iron chelating efficacy in vitro by two methods. First, by their ability to remove iron from ferritin in solution or second, to remove iron from iron-loaded hepatocytes in vitro. Our objective was to ascertain the importance of Kpart and pFe, on the biological efficiency of the molecule. Previous studies proposed that an ideal value of Kpart of 1 should give maximum biological activity. Mobilization of iron by Csox and CacCAM from ferritin was similar and furthermore more efficient than desferrioxamine B. In the iron-loaded hepatocyte cultures, the three hydroxyquinoline chelators, although showing diversity in terms of lipophilicity, appeared to be very similar in their capacity to chelate iron. CacCAM, the unique catecholate, was the most efficient of the molecules tested, as well as being the least toxic in the cellular model despite having the lowest value of pFe. In conclusion, the use of the partition coefficient and pFe, as tools for predicting biological activity of iron chelators should be not generalized. Further studies are required in order to understand the influence of the structure on the biological activity of the molecule." @default.
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• W2068675344 date "2001-12-01" @default.
• W2068675344 modified "2023-10-18" @default.
• W2068675344 title "New 8-hydroxyquinoline and catecholate iron chelators: influence of their partition coefficient on their biological activity11Abbreviations: Kpart, partition coeffient; DFO, desferrioxamine B; TRX, O-Trensox; pFe = −log[Fe3+aq] at pH 7.4 with [Ligand] = 10 μM and [Fe] = 1 μM; LDH, lactate dehydrogenase; and PBS, phosphate-buffered saline." @default.
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• W2068675344 doi "https://doi.org/10.1016/s0006-2952(01)00779-1" @default.
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