DNA binding by analogues of the bifunctional intercalator TANDEM.

Hampshire, A..J., Rusling, D.A., Bryan, S., Paumier, D., Dawson, S.J., Malkinson, J.P., Searcey, M. and Fox, K.R. (2008) DNA binding by analogues of the bifunctional intercalator TANDEM. Biochemistry, 47 (30). pp. 7900-7906. 10.1021/bi800573p.

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DOI: 10.1021/bi800573p

Abstract

We have used DNase I footprinting to study the binding strength and DNA sequence selectivity of novel derivatives of the quinoxaline bis-intercalator TANDEM. Replacing the valine residues in the cyclic octadepsipeptide with lysines does not affect the selectivity for TpA but leads to a 50-fold increase in affinity. In contrast, replacing both of the quinoxaline chromophores with naphthalene rings abolishes binding, while changing a single ring decreases the affinity, and footprints are observed at only the best binding sites (especially TATATA). By using fragments with different lengths of [(AT) n ], we demonstrate that these ligands bind best to the center of the longer (AT) n tracts.

Item Type:Article
Departments, units and centres:Department of Pharmaceutical and Biological Chemistry > Department of Pharmaceutical and Biological Chemistry
ID Code:2979
Journal or Publication Title:Biochemistry
Deposited By:Library Staff
Deposited On:16 Mar 2012 09:48
Last Modified:16 Mar 2012 09:48

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