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The NAMI A - Human Ferritin System: A Biophysical Characterization

The NAMI A - Human Ferritin System: A Biophysical Characterization

Silvia Ciambellotti, Alessandro Pratesi, Mirko Severi, Giarita Ferraro, Enzo Alessio, Antonello Merlino, Luigi Messori

Dalton Trans. 2018 Aug 21;47(33):11429-11437.

PMID: 30063237

Abstract:

The reaction of the antimetastatic ruthenium(iii) drug NAMI A with human H-chain ferritin (HuHf) was investigated through a variety of biophysical methods. We observed that the addition of HuHf to NAMI A solutions significantly increases the rate of spontaneous NAMI A hydrolysis suggesting the occurrence of a direct metallodrug-protein interaction. The resulting hydrolyzed Ru species binds the protein mostly forming a relatively tight 1 : 1 ruthenium/ferritin (subunit) adduct that was then separated and characterized. Notably, this adduct shows a characteristic CD spectrum in the visible region, which is diagnostic of the existence of at least one protein bound ruthenium center. The crystal structure of this NAMI A/HuHf adduct was subsequently solved at 1.58 Å resolution; clear evidence is given for the selective binding of a single Ru ion to His105 of each subunit with concomitant release of all other original Ru ligands in agreement with previous observations. We also noted that NAMI A produces a partial inhibition of HuHf ferroxidase activity. The implications of the above results are discussed.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP201653761	NAMI-A		201653-76-1	Price

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