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Original Articles

DNA Interaction of the Imidazole-containing Lexitropsin ImPy: Titration Viscometric Study in Comparison to Netropsin

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Pages 847-855 | Received 24 Nov 1994, Published online: 21 May 2012

References and Footnotes

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  • For the two modes, (I) and (II), at r ⩽ 0.023 of strongest Nt interaction with the sodium salt of calf thymus DNA the sum of their numbers of sites remains constant during temperature variation (as is the case for the further modes (III), (IV) alone) but their ratio varies (10,5). This particular behavior of mode (I) and mode (II) DNA sites on Nt interaction, together with other evidence, suggest a correlation to bent and lessbent or unbent A-tract containing DNA segments, respectively, and the existence of a temperature dependent equilibrium between both DNA forms (5)
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  • For the Nt-ctDNA system, the structure of the binding sites below r = 0.005 is in an equilibrium with the structure of mode (I) binding sites. The Nt binding sites of mode (I) interaction most probably are comprised of bend-forming A-tracts, those for mode (II) of more or less unbent A-tracts (5)
  • An approximate estimation of the association constant K can be derived from such data curves measured atdifferent DNA concentrations on the basis of the following reasonable assumptions: Equal Δy values of the two different curves, despite different r1 values, reflect equal DNA conformational changes and, hence, an equal value of r. Secondly, intrinsic viscosity may be approximated by (lnηrel)/c. This procedure seems to be reasonable for the small viscosity changes observed for most non-intercalating ligands. This kind of K determination is a difference method. Therefore, increased accuracy could be expected by a choice of DNA concentrations differing to greater extend than in the present experiments, which were designed for good mode resolution. (Cf. the distamycin-DNA system in Figure 1 of ref. 17.)
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  • Different modes are separable means that the difference in the free energy of binding for “adjacent” modes must be of the order of magnitude of 2–3 kcal/mole (4) or/and a high binding cooperativity should exist
  • Luck , G. , Reinert , K. E. , Baguley , B. and Zimmer , Ch. 1987 . J. Biomolec. Str. & Dyn. , 4 : 1079 – 1094 .
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