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      Alkylation of human hemoglobin A0 by the antimalarial drug artemisinin.

      Febs Letters
      Alkylation, Antimalarials, chemistry, pharmacology, Artemisinins, Chromatography, High Pressure Liquid, Heme, Hemoglobin A, metabolism, Humans, Oxidation-Reduction, Oxyhemoglobins, Sesquiterpenes, Spectrometry, Mass, Electrospray Ionization

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          Abstract

          In vitro, the heme cofactor of human iron(II) hemoglobin was efficiently and quickly alkylated at meso positions by the peroxide-based antimalarial drug artemisinin, leading to heme-artemisinin-derived covalent adducts. This reaction occurred in the absence of any added protease or in the presence of an excess of an extra non-heme protein, or even when artemisinin was added to hemolysed human blood. This activation of artemisinin by the heme moiety of non-digested hemoglobin clearly indicates the high affinity of this drug for heme, and its efficient alkylating ability under very mild conditions.

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