The interaction specificity of peptides with DNA. Evidence of peptide β-sheet-DNA binding

Gabbay, Edmond J.; Adawadkar, P. D.; Kapicak, Lou; Pearce, S. W.; Wilson, W. David

doi:10.1021/bi00646a023

Cited by 38 publications

(20 citation statements)

References 35 publications

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“…In fact, Gabbay and co-workers, with reporter molecules and peptides containing small aromatic ring systems which could insert a part of their molecule into the bases of DNA (44)(45)(46)(47), suggested that several derivatives could produce a very different effect on helix length and viscosity. One possibility proposed is that these compounds cause a bending of the double helix favouring a partial intercalation and resulting in a slight decrease in length on complex formation.…”

Section: Discussionmentioning

confidence: 99%

Is the bithiazole moiety of bleomycin a classical intercalator?

Hénichart¹,

Bernier²,

Helbecque³

et al. 1985

Nucl Acids Res

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Bleomycin is a widespread anticancerous drug, the biological activity of which having been extensively studied. Its metal ion-chelating portion has been shown to cleave DNA whereas the role of the bithiazole moiety is still questionable. In order to elucidate this problem some 2',4-disubstituted bithiazoles structurally related to the "tripeptide S" moiety of bleomycin were synthesized and their interaction with DNA was studied using 4Tm, fluorescence, EPR and viscometry techniques. The results of ATm and fluorescence quenching determinations were in favour of a binding of the bithiazole part by an intercalation process. Nevertheless, the use of the spin-label probes indicated only a partial intercalation of the ring between the base-pairs. Moreover, viscometry data which clearly exhibited a slight decrease of DNA length in the presence of bithiazole derivative led to the proposal of a binding model involving a partial insertion of a thiazole ring which wedges in between the bases at a bending point of DNA.

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Section: Discussionmentioning

confidence: 99%

Is the bithiazole moiety of bleomycin a classical intercalator?

Hénichart¹,

Bernier²,

Helbecque³

et al. 1985

Nucl Acids Res

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“…Whether the indole ring is fully inserted between base pairs or partially inserted is still unknown. On the basis of physicochemical and viscosimetric studies, it was suggested that the stacking of tryptophan with bases could induce a bend in the DNA structure as a result of a partial insertion between successive base pairs (Gabbay et al, 1976; Héléne & Maurizot, 1981).…”

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confidence: 99%

Does tryptophan intercalate in DNA? A comparative study of peptide binding to alternating and non-alternating A.cntdot.T sequences

Rajeswari¹,

Montenay-Garestier²,

Hélène³

1987

Biochemistry

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The interactions of a tetrapeptide, lysyltryptophylglycyllysine tert-butyl ester (KWGK), with synthetic double-stranded polynucleotides [poly(dA).poly(dT), poly[d(A-T)], poly(rA).poly(dT), and poly(rA).poly(rU)], Escherichia coli DNA, and single-stranded polynucleotides [poly(rA), poly(rU), poly(dA), and poly(dT)] were studied in a low-salt buffer by absorption and fluorescence spectroscopy. From fluorescence quenching data, we determined the two binding constants K1 and K2 of the two-step mechanism previously proposed for lysyltryptophyllysine binding to polynucleotides [Brun, F., Toulmé, J.J., & Hélène, C. (1975) Biochemistry 14, 558-563]. The first complex (PN)1 is purely due to electrostatic interactions between the lysyl residues and the phosphate groups. The second complex (PN)2 involves an additional stacking of the indole moiety of the tryptophyl residue with the bases (or base pairs) of the polynucleotide and is in equilibrium with (PN)1. K2 measures the ratio of the concentrations of stacked and unstacked complexes. The fluorescence decay of the tryptophyl residue in KWGK was not significantly different in the presence and in the absence of double-stranded polynucleotides in agreement with the previous model, which assumes total quenching of tryptophan fluorescence in complex (PN)2 and identical fluorescence characteristics for free KWGK and complex (PN)1. The stacking of the tryptophyl residue with A.T base pairs in alternating poly[d(A-T)] was found to be 10 times more efficient than that with nonalternating poly(dA).poly(dT). Among A-T-containing double-stranded polynucleotides, poly(rA).poly(dT) was found to be the most favorable for tryptophan stacking. A similar behavior was previously demonstrated for several intercalating agents such as ethidium bromide, propidium iodide, and daunomycin.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…The results suggest that the c-and -amino groups of the N-terminal L-lysyl residue interact stereospecifically with the DNA helix thus dictating the positioning of the aromatic ring of the C-terminal phenylalanine residue. In the accompanying paper (Gabbay et al, 1976), the interaction of several oligopeptides, 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 ter- The 1B NMR signal of the aromatic protons of L-Lys-L-PheA (1) and L-Lys-D-PheA (2) (a and b, respectively); in the absence (a) and presence of DNA at a base pair to peptide ratio of 7.5 (b), 3.6 (c), 2.4 (d), and 0.5 (e).…”

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confidence: 99%

Stereospecific binding of diastereomeric peptides to salmon sperm DNA

Gabbay¹,

Adawadkar²,

Wilson³

1976

Biochemistry

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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).

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The interaction specificity of peptides with DNA. Evidence of peptide β-sheet-DNA binding

Cited by 38 publications

References 35 publications

Is the bithiazole moiety of bleomycin a classical intercalator?

Is the bithiazole moiety of bleomycin a classical intercalator?

Does tryptophan intercalate in DNA? A comparative study of peptide binding to alternating and non-alternating A.cntdot.T sequences

Stereospecific binding of diastereomeric peptides to salmon sperm DNA

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