Stearylated arginine-rich peptides: a new class of transfection systems

Bioconjug Chem. Nov-Dec 2001;12(6):1005-11. doi: 10.1021/bc015508l.

Abstract

Membrane-permeable arginine-rich peptides, such as HIV-1 Tat-(48-60), HIV-1 Rev-(34-50), and flock house virus (FHV) coat-(35-49), have been shown to possess the ability to transfect COS-7 cells with luciferase-coding plasmid as efficiently as polyarginine (MW 5000-15 000) and polylysine (MW 9800). Not only these virus-derived cationic peptides but also oligoarginines of 4-16 residues were found to be able to transfect cells. In the case of the Tat, FHV, and octaarginine peptides, N-terminal stearylation of the peptides increases the transfection efficiency by approximately 100 times to reach the same order of magnitude as that of LipofectAMINE, one of the most efficient commercially available transfection agents. Also, a certain correlation was observed between the transfection efficiency of stearyl-(Arg)n peptides (stearyl-Rn: n = 4, 8, 12, 16) and the membrane permeability of the corresponding (Arg)n peptides (Rn).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arginine / chemistry*
  • Biological Transport
  • COS Cells
  • Gene Products, rev / chemistry
  • Gene Products, tat / chemistry
  • Humans
  • Luciferases / genetics
  • Luciferases / metabolism
  • Molecular Sequence Data
  • Nodaviridae / chemistry
  • Oligopeptides / chemistry
  • Peptide Fragments / chemistry
  • Peptides / chemistry*
  • Plasmids
  • Stearic Acids / chemistry*
  • Transfection / methods*
  • Viral Proteins / chemistry
  • tat Gene Products, Human Immunodeficiency Virus

Substances

  • Gene Products, rev
  • Gene Products, tat
  • Oligopeptides
  • Peptide Fragments
  • Peptides
  • Stearic Acids
  • Viral Proteins
  • tat Gene Products, Human Immunodeficiency Virus
  • tat peptide (32-72), Human immunodeficiency virus 1
  • polyarginine
  • stearic acid
  • arginyl-glycyl-aspartic acid
  • Arginine
  • Luciferases