Effect on ribonucleotide reductase of novel lipophilic iron chelators: the desferri-exochelins. Biochem Biophys Res Commun 2004 Mar 12;315(3):595-8
Date
02/21/2004Pubmed ID
14975742DOI
10.1016/j.bbrc.2004.01.101Scopus ID
2-s2.0-1242295296 (requires institutional sign-in at Scopus site) 30 CitationsAbstract
Desferri-exochelins are siderophores secreted by Mycobacterium tuberculosis that are both lipid- and water-soluble and have a high binding affinity for iron. Desferri-exochelin 772SM inhibits DNA replication and ribonucleotide reductase activity at 10-fold less concentration than the lipid-insoluble iron chelator deferoxamine, which is currently in clinical use. Neither chelator can extract iron directly from ribonucleotide reductase. However, because of its lipid-solubility and high binding affinity, desferri-exochelin is able to enter cells rapidly and access intracellular iron, while deferoxamine has limited capacity to cross the cell membrane.
Author List
Hodges YK, Antholine WE, Horwitz LDMESH terms used to index this publication - Major topics in bold
Breast NeoplasmsCell Line, Tumor
DNA
DNA Replication
Deferoxamine
Electron Spin Resonance Spectroscopy
Enzyme Inhibitors
Free Radicals
Humans
Hydrophobic and Hydrophilic Interactions
Iron Chelating Agents
Peptides, Cyclic
Ribonucleotide Reductases
Tyrosine
