Molecular complexes of quinoline antimalarials with iron-porphyrin components of protease-digested methemoglobin.
Chloroquine, quinine, mefloquine and quinacrine have been found by difference spectroscopy to interact with hemozoin from Plasmodium berghei, trypsin and pronase-digested methemoglobin, hemin, heme, protoporphyrin IX and hematoporphyrin. These drugs also compete with one another in their binding to hemin. It is proposed that the iron-porphyrin moiety of digested hemoglobin is a common binding site for the accumulation of the schizontocidal drugs in the autophagosomes of the malarial parasite.
D000818:Animals; D000962:Antimalarials / Q000378:metabolism*; D001665:Binding Sites; D002417:Cattle; D006418:Heme / Q000378:metabolism*; D006801:Humans; D006868:Hydrolysis; D008706:Methemoglobin / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism; D011485:Protein Binding; D011804:Quinolines / Q000378:metabolism*
D000962:Antimalarials; D011804:Quinolines; D006418:Heme; D008706:Methemoglobin; D010447:Peptide Hydrolases