Calorimetric investigation of ethidium and netropsin binding to chicken erythrocyte chromatin

Biochemistry
A TaquetC Houssier

Abstract

We have investigated the thermodynamic aspects of the ligand binding to chromatin, using isothermal titration calorimetry. Two classical DNA ligands were used: an intercalator, ethidium bromide, and a minor groove binder, netropsin. Stoichiometry, affinity constant, and thermodynamic parameters were determined at various salt concentrations and different temperatures. The effect of ionic strength was analyzed according to the Record theory applied to chromatin. We also compared the binding parameters on naked DNA, H1/H5-depleted chromatin, and chromatin. We demonstrated that the presence of histones on DNA still allows the ligand binding that takes place according to a simple one single-site model. For both ligand types, the thermodynamic driving force is enthalpic and the association is characterized by a somewhat weaker affinity and more scattered ligand distribution than on naked DNA. The ligand affinity is weakly altered by the salt-induced compaction of the chromatin and the binding is accompanied by a release of one counterion per ligand molecule. The temperature-dependent studies revealed the existence of a small heat capacity change associated with ligand binding to chromatin, together with an enthalpy-entropy compensat...Continue Reading

References

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Citations

Jul 4, 2012·Journal of Biosciences·Dipak DasguptaAmrita Banerjee
Jun 6, 2003·Bioorganic & Medicinal Chemistry·Mohd Ayoub MirDipak Dasgupta
Nov 3, 2011·PloS One·Parijat Majumder, Dipak Dasgupta
Mar 31, 2004·Canadian Journal of Physiology and Pharmacology·Liliana RaduB Constantinescu
Mar 22, 2014·FEBS Open Bio·Amrita BanerjeeDipak Dasgupta
May 12, 2015·Biochemical and Biophysical Research Communications·Amrita BanerjeeDipak Dasgupta

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