Design, synthesis, and biological activity of a cyclic peptide: an inhibitor of HIV-1 tat-TAR interactions in human cells

Bioorg Med Chem Lett. 2000 May 1;10(9):971-4. doi: 10.1016/s0960-894x(00)00140-2.

Abstract

Replication of human immunodeficiency virus type 1 (HIV-1) requires specific interactions of Tat protein with the transactivation responsive region (TAR) RNA, a 59-base stem-loop structure located at the 5'-end of all HIV mRNAs. A number of cyclic peptides are known to possess antibiotic activity and increased biological stability. Here we report the design, synthesis, and biological activity of a cyclic peptide (2), which inhibits transcriptional activation by Tat protein in human cells with an IC50 of approximately 40 nM. Cyclic peptides that can target specific RNA structures provide a new class of small molecules that can be used to control cellular processes involving RNA-protein interactions in vivo.

MeSH terms

  • Anti-HIV Agents / chemical synthesis*
  • Anti-HIV Agents / pharmacology
  • Cells, Cultured
  • Drug Design
  • Gene Expression Regulation, Viral / drug effects
  • Gene Expression Regulation, Viral / genetics
  • Gene Products, tat / antagonists & inhibitors*
  • HIV-1 / drug effects
  • HIV-1 / genetics
  • HIV-1 / metabolism
  • HeLa Cells
  • Humans
  • Ligands
  • Peptides, Cyclic / chemical synthesis*
  • Peptides, Cyclic / pharmacology
  • RNA, Viral / drug effects
  • Transcriptional Activation / drug effects
  • tat Gene Products, Human Immunodeficiency Virus

Substances

  • Anti-HIV Agents
  • Gene Products, tat
  • Ligands
  • Peptides, Cyclic
  • RNA, Viral
  • tat Gene Products, Human Immunodeficiency Virus