Structural Analysis of Covalent Peptide Dimers, Bis(pyridine-2-carboxamidonetropsin)(CH2)3–6, in Complex with 5′-TGACT-S′ Sites by Two-Dimensional NMR

Tammy J. Dwyer, Bernhard H. Geierstanger, Milan Mrksich, Peter B. Dervan, David E. Wemmer*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

57 Scopus citations

Abstract

The peptide pyridine-2-carboxamidonetropsin (2-PyN) binds specifically in the minor groove of 5′-(A,T)G-(A,T)C(A,T)-3′ sequences as a side-by-side antiparallel dimer. Tethering two 2-PyN ligands through the nitrogens of the central pyrrole rings with propyl, butyl, pentyl and hexyl linkers affords covalent peptide dimers, bis(pyridine-2-carboxamide-netropsin) (CH2)3-6, which bind in the minor groove of DNA with increased binding affinities and improved sequence specificities. Two-dimensional NMR studies of the complexes formed upon binding of these covalent peptide dimers to an oligonucleotide containing a 5′-TGACT-3′ site reveal that the dimeric peptides bind as intramolecular dimers with nearly identical geometry and peptide-DNA contacts as in the (2-PyN)2•-5′-TGACT-3′ complex.

Original languageEnglish (US)
Pages (from-to)9900-9906
Number of pages7
JournalJournal of the American Chemical Society
Volume115
Issue number22
DOIs
StatePublished - Nov 1 1993

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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