Structural variety of membrane permeable peptides

• Published in: Current protein & peptide science Vol. 4; no. 2; p. 87
• Main Authors: Futaki, Shiroh, Goto, Susumu, Suzuki, Tomoki, Nakase, Ikuhiko, Sugiura, Yukio
• Format: Journal Article
• Language: English
• Published: United Arab Emirates 01.04.2003
• Subjects: Amino Acid Sequence; Amino Acids, Branched-Chain - chemistry; Amino Acids, Branched-Chain - metabolism; Animals; Arginine - chemistry; Arginine - metabolism; Cell Membrane Permeability; Gene Products, rev - chemical synthesis; Gene Products, rev - chemistry; Gene Products, rev - metabolism; Gene Products, tat - chemistry; Gene Products, tat - metabolism; HeLa Cells; HIV-1 - chemistry; HIV-1 - metabolism; Humans; Peptide Fragments - chemistry; Peptide Fragments - metabolism; Peptides - chemical synthesis; Peptides - chemistry; Peptides - classification; Peptides - metabolism; Protein Transport; rev Gene Products, Human Immunodeficiency Virus; Structure-Activity Relationship; tat Gene Products, Human Immunodeficiency Virus
• ISSN: 1389-2037
• DOI: 10.2174/1389203033487261

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 approximately 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.