Conjugation of cell-penetrating peptides leads to identification of anti-HIV peptides from matrix proteins

Bioorg Med Chem. 2012 Feb 15;20(4):1468-74. doi: 10.1016/j.bmc.2011.12.055. Epub 2012 Jan 2.

Abstract

Compounds which inhibit the HIV-1 replication cycle have been found amongst fragment peptides derived from an HIV-1 matrix (MA) protein. Overlapping peptide libraries covering the whole sequence of MA were designed and constructed with the addition of an octa-arginyl group to increase their cell membrane permeability. Imaging experiments with fluorescent-labeled peptides demonstrated these peptides with an octa-arginyl group can penetrate cell membranes. The fusion of an octa-arginyl group was proven to be an efficient way to find active peptides in cells such as HIV-inhibitory peptides.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Anti-HIV Agents / chemistry*
  • Anti-HIV Agents / pharmacokinetics
  • Anti-HIV Agents / pharmacology*
  • Cell Membrane Permeability
  • Cell-Penetrating Peptides / chemistry*
  • Cell-Penetrating Peptides / genetics
  • Circular Dichroism
  • HIV / drug effects*
  • HeLa Cells
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Library*

Substances

  • Anti-HIV Agents
  • Cell-Penetrating Peptides
  • Peptide Library