On the interaction of oligopeptides containing aromatic amino acids with DNA in aqueous solution

Quadrifoglio, Franco; Giancotti, Vincenzo; Crescenzi, V.

doi:10.1016/0014-5793(76)80143-3

Cited by 10 publications

(1 citation statement)

References 16 publications

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“…Такое тушение наблюдается в комплексах с нуклеиновыми кислотами тирозин-содержащих пептидов типа Lys-Tyr-Lys [38][39][40], поли(Lys-Tyr) [41], гистона Hl [42,43], октамера гистонов [44,45], а также в нативных кор-частицах нуклеосом [46,47]. По данным ЯМР-спектроскопии [38,39] и калориметрических измерений [48], тирозил в составе трипептидов Lys-Tyr-Lys, в отличие от триптофанила, не способен к заметной интеркаляции между основаниями ДНК. Тушение флюоресценции таких трипептидов в комплексе с ДНК нельзя объяснить также образованием водородной связи между тирозином и компонентами нуклеиновых кислот [39].…”

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Fluorescence spectroscopy in the investigations of protein-nucleic acids interactions in chromatin

Sivolob

Khrapunov

1992

Biopolym. Cell

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Fluorescence spectroscopy in the investigations of protein-nucleic acids interactions in chromatin

Sivolob

Khrapunov

1992

Biopolym. Cell

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Specificity of DNA–basic polypeptide interactions. III. Sequential and random copolymers of lysine and aromatic amino acids

1979

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SynopsisSequential and random lysine copolymers containing various amounts of different aromatic amino acids were synthesized. The sequential copolypeptides exhibited strong dependence of yield and degree of polymerization on the amino acid sequence of the repeating unit. To elucidate the specific contributions of aromatic side chains to the interaction of these copolymers with DNA, direct-mixed complexes were studied by thermal denaturation and CD. The melting behavior of peptide-bound DNA was found to be strongly affected by amino acid composition and sequence. The CD spectrum of DNA was altered by random copolymers, whereas sequential copolymers exhibited no changes. The influence of the random copolymers on the CD spectrum of DNA decreased in the series: polylysine > [Lys,Phe], > [Lys,(OMe)Tyr], > [Lys,Tyr].. The contribution of the different aromatic amino acids to thermal stability is interpreted as stacking tendencies toward denatured and, in the case of Tyr, H-bond formation with native DNA. The differences found for the random and the sequential polypeptides can best be explained by assuming a cooperative action of rather small peptide segments.

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4.10.2.5 Enthalpy- and entropy-changes from calorimetric and van’t Hoff analysis

Pörschke¹

Landolt-Börnstein - Group VII Biophysics

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On the interaction of oligopeptides containing aromatic amino acids with DNA in aqueous solution

Cited by 10 publications

References 16 publications

Fluorescence spectroscopy in the investigations of protein-nucleic acids interactions in chromatin

Fluorescence spectroscopy in the investigations of protein-nucleic acids interactions in chromatin

Specificity of DNA–basic polypeptide interactions. III. Sequential and random copolymers of lysine and aromatic amino acids

4.10.2.5 Enthalpy- and entropy-changes from calorimetric and van’t Hoff analysis

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