The DNA-bound orientation of Cu(II)-Xaa-Gly-His metallopeptides.
The DNA-bound orientations of Cu(II) x Xaa-Gly-L-His metallopeptides (where Xaa is Gly, L-Lys or L-Arg) were investigated by DNA fiber EPR spectroscopy and molecular modeling. Observed and calculated EPR spectra indicated that the g// axes of 1:1 Cu(II) complexes of the tripeptides tilted about 50 degrees from the DNA fiber axis. These results suggest that the complexes are stereospecifically oriented in the DNA minor groove. Although the side chain of the N-terminal amino acid residue did not affect the orientation of the DNA-bound complexes, it contributed to their stability in the presence of DNA; the Cu(II) complex of Gly-Gly-L-His was found to dissociate to hydrated Cu(II) ion more extensively than the respective L-Lys-Gly-L-His and L-Arg-Gly-L-His complexes. The ionic interaction between the positively charged lysine or arginine residues and the negatively charged DNA phosphodiester backbone may result in the reduced dissociation of these complexes when bound to the DNA minor groove.
Nagane
R
R
Department of Applied Chemistry. Graduate School of Science and Engineering, Chuo University, Tokyo, Japan.
Koshigoe
T
T
Chikira
M
M
Long
E C
EC
D003300:Copper / Q000737:chemistry*; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D008667:Metalloproteins / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D008667:Metalloproteins; D010455:Peptides; D003300:Copper; D004247:DNA