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Alkylation of Microperoxidase‐11 by the Antimalarial Drug Artemisinin
Author(s) -
Rodriguez Montserrat,
Claparols Catherine,
Robert Anne,
Meunier Bernard
Publication year - 2002
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20021104)3:11<1147::aid-cbic1147>3.0.co;2-8
Subject(s) - artemisinin , heme , chemistry , moiety , combinatorial chemistry , yield (engineering) , alkylation , drug discovery , drug , biochemistry , stereochemistry , plasmodium falciparum , malaria , biology , pharmacology , catalysis , enzyme , immunology , materials science , metallurgy
Heading for heme : Alkylation of heme by the antimalarial drug artemisinin occurs in high yield, even when the heme moiety is still partially protected by a protein fragment (see scheme). Mass spectrometry revealed that microperoxidase‐II can be mono‐, di‐, and trialkylated by a carbon‐centered radical derived from the drug. This result indicates that complete digestion of globin in malaria‐infected erythrocytes may not be required for heme‐induced activation of artemisinin.