page_title: Ruthenium anti-cancer drugs
section_title: Transferrin transportation
hierarchical_section_title: Ruthenium anti-cancer drugs / Properties of ruthenium complexes / Transferrin transportation
caption_attribution_description: English: Cartoon representation of the molecular structure of protein registered with 1oqh code. Deutsch: Grafik des Molekularstruktur von jenem Protein, das mit 1oqh code registriert ist. Plattdüütsch: Grafik, de de Molekularstruktur von dat Protein wiest, dat mit’n Kood 1oqh registreert is.
context_page_description: Ruthenium anti-cancer drugs are coordination complexes of ruthenium complexes that have anticancer properties. They promise to provide alternatives to platinum-based drugs for anticancer therapy. No ruthenium anti-cancer drug has been commercialized.
  Since 1979, when Cisplatin entered clinical trials, there has been continuing interest in alternative metal-based drugs. The leading ruthenium-based candidates are NAMI-A and KP1019. The first one to enter was NAMI-A. More ruthenium drugs are still under development. Ruthenium complexes as anticancer drugs are almost always designed to mimic platinum drugs, for targeting DNA.
context_section_description: As ruthenium is in the same group as iron, they share many characteristics. Electronically, ruthenium molecules readily bond with nitrogen and sulphur donor molecules that are abundantly found in many proteins within the body. For this reason ruthenium complexes are able to take advantage of the body’s ability to efficiently transport and uptake of iron. The ruthenium complexes can be transported by binding to serum albumin and transferrin proteins. These proteins allow for the efficient uptake of soluble iron for metabolic purposes. As rapidly dividing cells have an increased demand for iron, the levels of transferrin receptors found on these cancerous cells are greatly increased. The receptor increase on cancerous cells has been document as two to twelve times that of healthy cells. This greatly increases the selectivity of the drug as the majority of the dose is sequestered in cancerous tissues, bypassing most healthy cells. This effect contributes to the lower toxicity that is associated to the ruthenium drugs in comparison to platinum. It is important to note that the ruthenium is not necessarily replacing the iron within these proteins, but that they are transported concurrently. It has been documented that transferrin-mediated ruthenium uptake is more efficient when the proteins are also saturated with iron.
caption: 3D rendering of a transferrin molecule
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