Generic placeholder image

Current Protein & Peptide Science

Editor-in-Chief

ISSN (Print): 1389-2037
ISSN (Online): 1875-5550

Structural Variety of Membrane Permeable Peptides

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

Volume 4, Issue 2, 2003

Page: [87 - 96] Pages: 10

DOI: 10.2174/1389203033487261

Price: $65

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.

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


Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy