Structural Variety of Membrane Permeable Peptides

Title: Structural Variety of Membrane Permeable Peptides

Volume: 4 Issue: 2

Author(s): Shiroh Futaki, Susumu Goto, Tomoki Suzuki, Ikuhiko Nakase and Yukio Sugiura

Affiliation:

Keywords: Peptide-mediated protein, human immunodeficient virus, arginine-rich peptides, macromolecules

Abstract: Peptide-mediated protein delivery into living cells has been attracting our attention. Among the peptides that have been reported to have carrier activity, the one from the human immunodeficient virus (HIV)-1 Tat has been most often used for the introduction of exogenous macromolecules into cells. We have shown that not only the Tat peptide, but also various arginine-rich peptides showed very similar characteristics in translocation, and the possible presence of ubiquitous internalization mechanisms among the arginine-rich peptides has also been suggested. These arginine-rich peptides includes ones derived from HIV-1 Rev and flock house virus coat proteins. The linear- and branched-chain peptides containing ∼8 residues of arginine also show a similar ability. In this review, we present the structural variety of membrane permeable peptides and provide a survey of the findings on the translocation of these peptides through the cell membranes.

Cite this article as:

Futaki Shiroh, Goto Susumu, Suzuki Tomoki, Nakase Ikuhiko and Sugiura Yukio, Structural Variety of Membrane Permeable Peptides, Current Protein & Peptide Science 2003; 4 (2) . https://dx.doi.org/10.2174/1389203033487261