Design of artificial transcriptional activators with rigid poly-L-proline linkers

Paramjit S. Arora, Aseem Z. Ansari, Timothy P. Best, Mark Ptashne, Peter B. Dervan

Research output: Contribution to journalArticlepeer-review


Typical eukaryotic transcriptional activators are composed of distinct functional domains, including a DNA binding domain and an activating domain. Artificial transcription factors have been designed wherein the DNA binding domain is a minor groove DNA binding hairpin polyamide linked by a flexible tether to short activating peptides, typically 16-20 residues in size. In this study, the linker between the polyamide and the peptide was altered in an incremental fashion using rigid oligoproline "molecular rulers" in the 18-45 Å length range. We find that there is an optimal linker length which separates the DNA and the activation region for transcription activation.

Original languageEnglish (US)
Pages (from-to)13067-13071
Number of pages5
JournalJournal of the American Chemical Society
Issue number44
StatePublished - Nov 6 2002

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry


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