Arginine-rich peptides: potential for intracellular delivery of macromolecules and the mystery of the translocation mechanisms

Int J Pharm. 2002 Oct 1;245(1-2):1-7. doi: 10.1016/s0378-5173(02)00337-x.

Abstract

A basic peptide derived from the human immunodeficiency virus (HIV)-1 Tat has been reported to have the ability to translocate through the cell membranes and to bring exogenous proteins into the cells. We have demonstrated that these features were observable among many arginine-rich peptides including those having a branched chain structure. Based on these findings, the presence of a ubiquitous internalization mechanism for the arginine-rich peptides has been suggested. In this review, the potential of these peptides for the intracellular delivery of macromolecules and the mystery of the translocation mechanisms are reviewed.

Publication types

  • Review

MeSH terms

  • Amino Acid Substitution
  • Animals
  • Arginine / genetics*
  • Cell Membrane / metabolism
  • Cell Nucleus / metabolism
  • Drug Carriers
  • Endocytosis
  • Gene Products, tat / administration & dosage*
  • Gene Products, tat / genetics*
  • Gene Products, tat / metabolism
  • HIV-1
  • Humans
  • Peptide Fragments / administration & dosage*
  • Peptide Fragments / genetics*
  • Peptide Fragments / metabolism
  • tat Gene Products, Human Immunodeficiency Virus

Substances

  • Drug Carriers
  • Gene Products, tat
  • Peptide Fragments
  • tat Gene Products, Human Immunodeficiency Virus
  • tat peptide (48-60), Human immunodeficiency virus 1
  • Arginine