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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.

Type

Journal article

Journal

Anticancer Drug Des

Publication Date

12/2000

Volume

15

Pages

431 - 439

Keywords

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