An α-helical peptidomimetic inhibitor of the HIV-1 Rev-RRE interaction

Nicholas L. Mills, Matthew D. Daugherty, Alan D. Frankel, R. Kiplin Guy

Research output: Contribution to journalArticlepeer-review

48 Scopus citations


The interaction between the HIV-1 Rev protein and the Rev-Responsive Element (RRE) RNA is an attractive target for anti-viral therapy. We have designed α-helical peptidomimetics of Rev-like peptides using side chain-side chain macrolactam formation between positions i and i+4. One peptidomimetic having an appropriate location, orientation, and length of the macrolactam exhibited both significant helical character and specific RRE binding. This molecule displays 2-fold greater RNA specificity than the wild-type Rev peptide and more than 20-fold greater specificity than an uncyclized control peptide. Thus, specific, high affinity recognition of the RRE is feasible utilizing a small, relatively rigid peptidomimetic scaffold.

Original languageEnglish
Pages (from-to)3496-3497
Number of pages2
JournalJournal of the American Chemical Society
Issue number11
StatePublished - Mar 22 2006

ASJC Scopus subject areas

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


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