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DNA binding by analogues of the bifunctional intercalator TANDEM

DNA binding by analogues of the bifunctional intercalator TANDEM
DNA binding by analogues of the bifunctional intercalator TANDEM
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.
0006-2960
7900-7906
Hampshire, Andrew J.
68aac3b7-88b7-4417-8793-9c2a06b01abc
Rusling, David A.
d08f1f97-f8a9-4980-a025-ae41c23a938f
Bryan, Stephanie
8c195aed-24d0-465c-b689-e08a5b76c591
Paumier, David
73b2a6fe-881e-43f8-9bfd-e33a1d82a665
Dawson, Simon J.
b4f4fc55-7c16-467b-88d6-5754e172c87a
Malkinson, John P.
a8f447bf-dc3e-48f6-8129-8aebd348ee73
Searcey, Mark
92a85b46-a185-4c99-b12d-0e763be6549e
Fox, Keith R.
9da5debc-4e45-473e-ab8c-550d1104659f
Hampshire, Andrew J.
68aac3b7-88b7-4417-8793-9c2a06b01abc
Rusling, David A.
d08f1f97-f8a9-4980-a025-ae41c23a938f
Bryan, Stephanie
8c195aed-24d0-465c-b689-e08a5b76c591
Paumier, David
73b2a6fe-881e-43f8-9bfd-e33a1d82a665
Dawson, Simon J.
b4f4fc55-7c16-467b-88d6-5754e172c87a
Malkinson, John P.
a8f447bf-dc3e-48f6-8129-8aebd348ee73
Searcey, Mark
92a85b46-a185-4c99-b12d-0e763be6549e
Fox, Keith R.
9da5debc-4e45-473e-ab8c-550d1104659f

Hampshire, Andrew J., Rusling, David A., Bryan, Stephanie, Paumier, David, Dawson, Simon J., Malkinson, John P., Searcey, Mark and Fox, Keith R. (2008) DNA binding by analogues of the bifunctional intercalator TANDEM. Biochemistry, 47 (30), 7900-7906. (doi:10.1021/bi800573p). (PMID:18597492)

Record type: Article

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.

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Published date: 29 July 2008

Identifiers

Local EPrints ID: 142573
URI: http://eprints.soton.ac.uk/id/eprint/142573
ISSN: 0006-2960
PURE UUID: f45566ae-6072-4867-88d9-b6c007b655b2
ORCID for David A. Rusling: ORCID iD orcid.org/0000-0002-7442-686X
ORCID for Keith R. Fox: ORCID iD orcid.org/0000-0002-2925-7315

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Date deposited: 01 Apr 2010 15:42
Last modified: 14 Mar 2024 02:33

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Contributors

Author: Andrew J. Hampshire
Author: David A. Rusling ORCID iD
Author: Stephanie Bryan
Author: David Paumier
Author: Simon J. Dawson
Author: John P. Malkinson
Author: Mark Searcey
Author: Keith R. Fox ORCID iD

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