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Nucleic Acids Research, 2003, Vol. 31, No. 21 6191-6197
© 2003 Oxford University Press

Energetics of echinomycin binding to DNA

Fenfei Leng, Jonathan B. Chaires1 and Michael J. Waring*,2

Department of Chemistry, Florida International University, 11200 SW 8th Street, Miami, FL 33199, USA, 1 Department of Biochemistry, University of Mississippi Medical Center, Jackson, MS 39216-4505, USA and 2 Department of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge CB2 1PD, UK

*To whom correspondence should be addressed. Tel: +44 1223 334034; Fax: +44 1223 334040; Email: mjw11{at}cam.ac.uk
This paper is dedicated to the memory of Claude Hélène; a great scientist, respected scholar and valued friend

Differential scanning calorimetry and UV thermal denaturation have been used to determine a complete thermodynamic profile for the bis-intercalative interaction of the peptide antibiotic echinomycin with DNA. The new calorimetric data are consistent with all previously published binding data, and afford the most rigorous and direct determination of the binding enthalpy possible. For the association of echinomycin with DNA, we found {Delta}G° = –7.6 kcal mol–1, {Delta}H = +3.8 kcal mol–1 and {Delta}S = +38.9 cal mol–1 K–1 at 20°C. The binding reaction is clearly entropically driven, a hallmark of a process that is predominantly stabilized by hydrophobic interactions, though a deeper analysis of the free energy contributions suggests that direct molecular recognition between echinomycin and DNA, mediated by hydrogen bonding and van der Waals contacts, also plays an important role in stabilizing the complex.


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