Key result
Divalent metal-ion binding to the phosphonate group of (Dien)Pt(PMEA-N1) and (Dien)Pt(PMEA-N7) is only moderately inhibited by the twofold positively charged (Dien)Pt2+ unit at the adenine residue.
The study demonstrates that metal ion binding to the phosphonate group of PMEA is only moderately inhibited by a positively charged platinum unit, suggesting that multiple metal ions can participate in enzymatic processes involving nucleotides without serious charge repulsion.
No takes yet. Share an insight, caveat, or question.
Multiple metal ions may bind nucleotide analogs without major repulsion; leaves open enzymatic and therapeutic implications.
Kampf et al. (2001) studied this question. (Dien)Pt(PMEA-N1) and (Dien)Pt(PMEA-N7) complexes vs. M(PMEA) complexes was evaluated on Acidity and stability constants. Divalent metal-ion binding to the phosphonate group of (Dien)Pt(PMEA-N1) and (Dien)Pt(PMEA-N7) is only moderately inhibited by the twofold positively charged (Dien)Pt2+ unit at the adenine residue.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: