Stereospecific binding of diastereomeric peptides to salmon sperm DNA.

Studies of the interaction specificities of L-lysyl-L-phenylalaninamide (1) and the diastereomeric dipeptide amide, L-lysyl-D-phenylalaninamide (2), with salmon sperm DNA reveal distinct differences in the binding site of the aromatic ring of the phenylalanine residue. The results of 1H nuclear magnetic resonance (NMR), spin-lattice relaxation rates, viscometric, and flow dichroism studies indicate the aromatic ring of 1 is "partially" inserted between base pairs of DNA whereas the aromatic ring of 2 points outward toward the solution. The terminal L-lysyl residue presumably interacts stereospecifically with DNA helix thus dictating the positioning of the aromatic ring of the C-terminal phenylalanine residue. In the accompanying paper (E. J. Gabbay et al. (1976), Biochemistry, following paper in this issue), the interaction of several oligopeptide amides (containing the N-terminal L-Lys-L-Phe residue) with DNA is examined. The results are found to be consistent with stereospecific binding of the terminal L-lysyl residue, and in addition, the evidence suggests that oligopeptides may bind to DNA via a modified single-stranded beta-sheet structure which is wrapped around the nucleic acid helix in a manner similar to that described by M. H. F. Wilkins (1956), Cold Spring Harbor Symp. Quant. Biol. 21, 75).

[1]  O. Jardetzky,et al.  Introduction to magnetic resonance spectroscopy methods and biochemical applications. , 2006, Methods of biochemical analysis.

[2]  W. Wilson,et al.  Letter: Stereospecific interaction of dipeptide amides with DNA. Evidence for partial intercalation and bending of the helix. , 1975, Journal of the American Chemical Society.

[3]  E. Gabbay,et al.  Effect of aromatic cations on the tertiary structure of deoxyribonucleic acid. , 1975, Journal of the American Chemical Society.

[4]  J. Dimicoli,et al.  Interactions of aromatic residues of proteins with nucleic acids. I. Proton magnetic resonance studies of the binding of tryptophan-containing peptides to poly(adenylic acid) and deoxyribonucleic acid. , 1974, Biochemistry.

[5]  C. Baxter,et al.  Specific interaction of peptides with nucleic acids. Evidence for a "selective bookmark" recognition hypothesis. , 1973, Biochemistry.

[6]  C. Baxter,et al.  Specific interaction of peptides with nucleic acids. , 1972, Biochemistry.

[7]  T. Montenay-Garestier,et al.  Interactions of tyrosine and tyramine with nucleic acids and their components. Fluorescence, nuclear magnetic resonance and circular dichroism studies. , 1971, Biochimica et biophysica acta.

[8]  J. Dimicoli,et al.  Binding of tryptamine and 5-hydroxytryptamine (serotonin) to nucleic acids. Fluorescence and proton magnetic resonance studies. , 1971, Biochemistry.

[9]  P. Ts'o,et al.  Interaction of poly-L-tyrosine with nucleic acids. I. Formation of complexes. , 1971, Biochemistry.

[10]  M. Mandel,et al.  Interaction of aromatic amino acids with neutral polyadenylic acid. , 1971, Proceedings of the National Academy of Sciences of the United States of America.

[11]  P. E. Brown.  The interaction of basic dipeptide methyl esters with DNA. , 1970, Biochimica et biophysica acta.

[12]  G. W. Anderson,et al.  A reinvestigation of the mixed carbonic anhydride method of peptide synthesis. , 1967, Journal of the American Chemical Society.

[13]  D M Crothers,et al.  Studies of the binding of actinomycin and related compounds to DNA. , 1968, Journal of molecular biology.

[14]  M. Wilkins.  Physical studies of the molecular structure of deoxyribose nucleic acid and nucleoprotein. , 1956, Cold Spring Harbor symposia on quantitative biology.