Elsamicin A binding to DNA. A comparative thermodynamic characterization

  title={Elsamicin A binding to DNA. A comparative thermodynamic characterization},
  author={Francisca Barcel{\'o} and Jos{\'e} Portugal},
  journal={FEBS Letters},
Thermal analysis of ligand-DNA interaction: determination of binding parameters
The review discusses the methods of thermodynamic analysis of reactions of non-covalent binding of biologically active compounds with DNA, which is a key constituent of cell chromatin, and methods utilizing the Ising-type models and models based on the equations of chemical equilibrium.
Studies on the binding ability of diclofenac sodium to cationic surfactants micelles in aqueous ethanol solutions
Binding of diclofenac sodium (DCF), a non-steroidal anti-inflammatory drug, to hexadecyltrimethylammonium bromide and tetradecyltrimethylammonium bromide micelles in water as well as in aqueous
Insights into the binding of the drugs diclofenac sodium and cefotaxime sodium to serum albumin: calorimetry and spectroscopy.
Survey of the year 2005: literature on applications of isothermal titration calorimetry
An overview of the literature for 2005 is attempted to highlight works of interest and novelty and draw attention to those works which it is felt have provided a route to better analysis and increased the ability to understand the meaning of thermodynamic change on binding.
Master Author Index


Thermodynamic characterization of the multivalent binding of chartreusin to DNA.
A detailed thermodynamic profile is obtained for the interaction of this multivalent drug, which makes possible a dissection of DeltaG(obs) into the component free energy terms.
Chartreusin, elsamicin A and related anti-cancer antibiotics.
  • J. Portugal
  • Chemistry, Biology
    Current medicinal chemistry. Anti-cancer agents
  • 2003
Chartreusin and elsamicin A are structurally related antibiotics that bind to GC-rich tracts in DNA, with a clear preference for B-DNA over Z-DNA. They inhibit RNA synthesis and cause single-strand
Selective DNA cleavage by elsamicin A and switch function of its amino sugar group.
The present results indicate that guanine-specific recognition and selective cleavage of DNA by the antitumor antibiotic elsamicin A equipped with an amino sugar and compare these results with cleavage by chartarin and chartreusin antibiotics and found that an acetylation of the amino group on the elsamsicin A sugar portion plays an interesting switch function for the activity of elsamyin A.
Molecular dynamics study of the binding of elsamicin A to DNA.
Molecular mechanics and dynamics were used to examine the conformational flexibility of elsamicin A, an antitumour antibiotic, in aqueous solution and obtained the first three-dimensional model of the el samicin-A-DNA complex.
Dissecting the free energy of drug binding to DNA.
  • J. Chaires
  • Chemistry, Biology
    Anti-cancer drug design
  • 1996
Advances in polyelectrolyte theory have provided a simple and straightforward basis for dissecting the free energy of ligand binding to DNA into its polyelectrolyte and non-electrostatic
Parsing the free energy of anthracycline antibiotic binding to DNA.
The results and analysis presented here provide a rigorous and detailed description of structure-DNA affinity relationships among anthracycline antibiotics and will be useful in the formulation of rules for the rational design of novel DNA binding agents.
Energetics of DNA intercalation reactions.
Analysis showed that the DNA binding behavior of these simple intercalators is driven almost equally by hydrophobic effects and van der Waals contacts within the intercalation site.
Thermodynamics of drug-DNA interactions.
  • I. Haq
  • Biology, Chemistry
    Archives of biochemistry and biophysics
  • 2002