Interaction between the peptide lysyl‐tryptophanyl‐lysine and copolynucleotides of adenine and uracil: Selectivity of interaction

Maurizot, Jean‐Claude; Boubault, G.; Hélène, Claude

doi:10.1016/0014-5793(78)80600-0

Cited by 14 publications

(2 citation statements)

References 14 publications

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“…Among the different available sequences in a poly(A,C) the stacking interaction of Lys-Trp-Lys decreases in the order A A > AC and CC. A similar study with copolymers of adenine and uracil in single-stranded conformation has shown that the interaction is favored in UU sequence (Maurizot et al, 1978). Thus we have the following order of stacking interactions of the tryptophyl residue of Lys-Trp-Lys: UU > AU, AA > AC,CC.…”

Section: Discussionsupporting

confidence: 58%

Interaction of aromatic residues of proteins with nucleic acids. Binding of oligopeptides to copolynucleotides of adenine and cytosine

Maurizot¹,

Boubault²,

Hélène³

1978

Biochemistry

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The binding of the peptide Lys-Trp-Lys to various single-stranded copolymers of adenine and cytosine has been investigated using circular dichroism (CD) and fluorescence measurements. Two types of complexes are formed, both involving electrostatic interactions between lysyl residues and phosphate groups. The fluorescence quantum yield of the first complex is identical with that of the free peptide. The other complex involves a stacking of the polynucleotide bases with the tryptophan residue whose fluorescence is quenched. The binding of the peptide leads to a conformational change of the copolymers as shown by the CD variations. The fluorescence and CD data have been analyzed according to the model involving the two types of complexes. The values of the binding constants have been studied as a function of the cytosine content of the copolymers. Analysis of the stacking process in term of nearest neighbor frequency demonstrates that this binding is sequence dependent and is favored in AA sequence as compared with AC, CA, and CC sequence. Thus this simple tripeptide is able to distinguish between various base sequences in a single-stranded nucleic acid.

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Section: Discussionsupporting

confidence: 58%

Interaction of aromatic residues of proteins with nucleic acids. Binding of oligopeptides to copolynucleotides of adenine and cytosine

Maurizot¹,

Boubault²,

Hélène³

1978

Biochemistry

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“…According to Helene and coworkers, aromatic amino acids preferentially stack to single stranded nucleotide chains and do not stack to the same extent with double stranded polynucleotides.3'5 Moreover, Helene and coworkers found some specificity for the stacking of peptides containing tryptophane with single stranded polynucleotides. [6][7] Among the methods applied so far the NMR measurements provide the most detailed information about the complexes formed. The upfield shifts observed for the protons of Trp, Tyr and Phe upon binding to single stranded polynucleotides suggest the existence of a plane to plane contact between the aromatic ring systems of the amino acids and the nucleotide bases.…”

Section: Introductionmentioning

confidence: 99%

Structure and dynamics of a tryptophanepeptide-polynucleotide complex

Pörschke¹

1980

Nucl Acids Res

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The binding of LysTrpLys to single stranded poly(A) was studied by measurements of fluorescence, UV-absorbance, electrodichroism and field jump relaxation. The van't Hoff enthalpy determined at constant degree of peptide protonation is -3.5 kcal/mol (delta S = 9 e.u.). The electrodichroism of bound tryptophane residues is negative; its absolute value decreases with increasing degree of binding theta. The magnitude of the dichroism at low theta indicates a preferential orientation of the tryptophane residues in the plane of the adenine bases, suggesting stacking of Trp with adenine bases. The overall degree of orientation decreases, however, to virtually zero at high theta. Relaxation measurements by low theta demonstrate the existence of two steps in the binding reaction of LysTrpLys to poly(A): a fast bimolecular step controlled by diffusion is followed by a slow intramolecular conversion with a forward rate of 1.5 x 10(5) s-1 and a backward rate of 2.7 x 10(3) s-1. The forward rate is close to that expected for an insertion reaction into stacked poly(A), yet the corresponding stability constant (approximately 55) is unexpectedly high.

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Thermodynamische Messungen der Bindungsenthalpie kleiner Liganden mit Nukleinsäuren II. Anlagerung von Oligopeptiden an DNA

Burkart

Klump

1981

Ber Bunsenges Phys Chem

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W. Burkart und H. Klump: Thermodynamische Messungen der Bindungsenthalpien kleiner Liganden usw., I1 375 Hierbei ist AGilr die Anderung der freien Enthalpie bei der Bindung an einen isolierten Bindungsplatz und AGE, die Wechselwirkungen der Liganden untereinander. So 1aBt die Abnahme von AGie,,,, den SchluR zu, da AGilr unabhlngig vom Bindungsgrad ist, da8 unter den Liganden antikooperative Wechselwirkungen auftreten. Es ist plausibel, dalj der EinfluB von AG& mit wachsendem Bindungsgrad groBer wird. Der Vergleich der Ergebnisse der Untersuchungen mit den unterschiedlichen Methoden zeigt, dalj die spektroskopischen Methoden [ 101 und die kalorimetrischen Messungen grundsatzlich die gleichen Reaktionen erfassen. Es ist daher sehr zufriedenstellend, dalj sich unabhangig voneinander die gleichen thermodynamischen Parameter ergeben. Die ausfuhrliche Diskussion der einzelnen Beitrage, wie sie von Pauluhn und Zimmermann [lo] vorgenommen worden ist, IaBt sich auch auf die Ergebnisse der kalorimetrischen Messungen ausdehnen. Davon abweichend sind die Ergebnisse, die rnit Apurinsaure erhalten wurden. Dieser Polyelektrolytstrang zeigt aufgrund seiner hoheren Flexibilitat und seiner Unfahigkeit zur Intercalation einen komplexen Verlauf der thermodynamischen Parameter als Funktion der lurjeren Parameter Temperatur, Farbstoffkonzentration und Ionenstarke. Diese Arbeit wurde von der Deutschen Forschungsgemeinschaft unterstiltzt. Wir danken dem Leiter des Instituts fur Physikalische Chemie I1 der Universitat Freiburg, Herrn Prof. Th. Ackermann, fur seine wohlwollende FOrderung. Die sorgfaltige technische Assistenz von Frau Lehr verdient besondere Anerkennung. Die Zeichnungen wurden

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Interaction between the peptide lysyl‐tryptophanyl‐lysine and copolynucleotides of adenine and uracil: Selectivity of interaction

Cited by 14 publications

References 14 publications

Interaction of aromatic residues of proteins with nucleic acids. Binding of oligopeptides to copolynucleotides of adenine and cytosine

Interaction of aromatic residues of proteins with nucleic acids. Binding of oligopeptides to copolynucleotides of adenine and cytosine

Structure and dynamics of a tryptophanepeptide-polynucleotide complex

Thermodynamische Messungen der Bindungsenthalpie kleiner Liganden mit Nukleinsäuren II. Anlagerung von Oligopeptiden an DNA

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