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• W2072694788 abstract "13-Hydroxypyridin-4-ones are currently one of the main candidates for the development of orally active iron chelators. Small bidentate ligands tend to inhibit iron-containing metalloenzymes and therefore can cause undesirable side effects. A range of 3-hydroxypyridin-4-ones with different R2 substitutents was selected for the investigation of the structure–activity relationship between the chemical nature of the ligand and the inhibition of mammalian tyrosine hydroxylase. Results indicated that lipophilicity was the dominant factor in controlling the ability of this class of chelator to inhibit mammalian tyrosine hydroxylase. Ligands with hydrophilic R2 substitutents tended to be weak inhibitors. No significant correlation was found in this study between iron-binding affinity, extended R2 chain length, and enzyme inhibitory activity. In contrast, both the LogP values of the entire molecule and of the R2 segment correlated well with inhibitory activity." @default.
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• W2072694788 date "2001-02-01" @default.
• W2072694788 modified "2023-10-17" @default.
• W2072694788 title "Structure–activity investigation of the inhibition of 3-hydroxypyridin-4-ones on mammalian tyrosine hydroxylase" @default.
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• W2072694788 doi "https://doi.org/10.1016/s0006-2952(00)00551-7" @default.
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