¹H NMR Study of the Enantioselective Binding of λ- and Δ-[Ru(bpy)₂(m-bpy-GHK)]Cl₂ to the Deoxynucleotide Duplex d(5'-C₁G₂C₃G₄A₅A₆T₇T₈C₉G₁₀C₁₁G₁₂-3')₂

Abstract

The interaction of the diastereomeric complexes Λ- and Δ - [Ru(bpy)₂(m - GHK)]Cl₂, (GHK = glycine-histidine-lysine) to the deoxynucleotide duplex d(5'-CGCGAATTCGCG-3')₂ was studied by means of ¹H NMR spectroscopy. The diastereomers interact with the oligonucleotide duplex differently. The Δ - [Ru(bpy)₂ (m - GHK)]Cl₂ is characterized by major groove binding close to the central part of the oligonucleotide, with both the peptide and the bipyridine ligand of the complex involved in the binding. The λ - [Ru(bpy)₂ (m - bpy - GHK)]C₂ binds loosely, approaching the helix from the minor groove. The NMR analysis shows that the peptide (GHK) binding has a determinative role in the interactions of both diastereomers with the oligonucleotide.

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