Selenocysteine of thioredoxin reductase as the primary target for the antitumor metallodrugs: A computational point of view

Selenocysteine (Sec) has been recognized as a soft metal-coordinating residue that dues its relevance to the important role played in catalytic activity of thioredoxin reductase (TrxR), well-characterized anticancer target. Thus, several computational studies have devoted metalation this Se-based and metal scaffolds proposed potential Sec-binders, i.e. TrxR inhibitors. Here, we reported an overview chemical features Sec, well typical Sec-binding complexes, carried on metallodrugs primary target TrxR, by specifically posing our attention antitumour based Au(I), Au(III), Ag(I), Pt(II), Pt(IV), Ru(II), Ru(III), Rh(III) centers. Moreover, provided insight available structural data highlighted how optimal articulation methods modeling metallodrug-target system may expand understanding targeting active site metallic scaffolds.