par Goormaghtigh, Erik
;Huart, Pascal
;Praet, Michel;Brasseur, Robert
;Ruysschaert, Jean Marie 
Référence Biophysical chemistry, 35, 2-3, page (247-257)
Publication Publié, 1990




Référence Biophysical chemistry, 35, 2-3, page (247-257)
Publication Publié, 1990
Article révisé par les pairs
Résumé : | Adriamycin and its derivatives are among the most efficient antimitotics used in clinical therapy. A specific cardiotoxicity places a limit on the total dose of adriamycin that may be administered. The mechanism of cardiac toxicity is complex. Data accumulated from in vitro and in vivo studies indicate a possible common cause for the inhibition of numerous enzymes and tissue degradation by a free radical mechanism: the binding of adriamycin to the inner mitochondrial membrane cardiolipin. The structure of the adriamycin-cardiolipin complex has been investigated by using physico-chemical techniques and via conformational analysis. The results open a rational way to design new structures that are less cardiotoxic. |