1H NMR study of the enantioselective binding of lambda- and delta-[Ru(bpy)2(m-bpy-GHK)]Cl2 to the deoxynucleotide duplex d(5'-C1G2C3G4A5A6T7T8C9G10C11G12-3')2.
The interaction of the diastereomeric complexes Lambda- and Delta - [Ru(bpy)(2)(m - GHK)]Cl(2), (GHK = glycine-histidine-lysine) to the deoxynucleotide duplex d(5'-CGCGAATTCGCG-3')(2) was studied by means of (1)H NMR spectroscopy. The diastereomers interact with the oligonucleotide duplex differently. The Delta - [Ru(bpy)(2) (m - GHK)]Cl(2) 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 lambda - [Ru(bpy)(2) (m - bpy - GHK)]C(2) 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.
Myari
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Laboratory of Inorganic and General Chemistry, Department of Chemistry, University of Ioannnina, Ioannina 45110, Greece.
Hadjiliadis
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N
Garoufis
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A