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The antitrypanosomal and antitumour activities of (2,2':6',2"-terpyridine)platinum(II) complexes have been postulated to be due to their ability to inhibit irreversibly the NADPH/FAD redox enzymes trypanothione reductase and human thioredoxin reductase respectively. Here we show that these platinum(II) complexes metallate recombinant human albumin (rHA) at the single free thiol group (Cys-34). Moreover, the (2,2':6',2"-terpyridine)platinum(II) complex can be transferred from rHA to other thiols, such as 2-hydroxyethanethiol or glutathione. Human serum albumin could therefore provide a natural transport mechanism for the selective delivery of these agents to tumor cells by the enhanced permeability and retention (EPR) mechanism.


Journal article


Anticancer Drug Des

Publication Date





431 - 439


2,2'-Dipyridyl, Antineoplastic Agents, Biological Transport, Glutathione, Humans, Magnetic Resonance Spectroscopy, Organoplatinum Compounds, Recombinant Proteins, Serum Albumin, Spectrometry, Mass, Electrospray Ionization, Spectrophotometry, Ultraviolet, Sulfhydryl Compounds, Tumor Cells, Cultured