Membrane permeability commonly shared among arginine-rich peptides.
Delivery of proteins and other macromolecules using membrane-permeable carrier peptides is a recently developed novel technology, which enables us to modulate cellular functions for biological studies with therapeutic potential. One of the most often used carrier peptides is the arginine-rich basic peptide derived from HIV-1 Tat protein [HIV-1 Tat (48-60)]. Using this peptide, efficient intracellular delivery of molecules including proteins, oligonucleic acids and liposomes has been achieved. We have demonstrated that these features were commonly shared among many arginine-rich peptides such as HIV-1 Rev (34-50) and octaarginine. Not only the linear peptides but also branched-chain peptides showed efficient internalization with an optimum number of arginines (approximately eight residues). The structural and mechanistic features of the translocation of these membrane-permeable arginine-rich peptides are reviewed.
Futaki
Shiroh
S
Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan. futaki@scl.kyoto-u.ac.jp
Goto
Susumu
S
Sugiura
Yukio
Y
D001120:Arginine / Q000378:metabolism*; D001693:Biological Transport, Active; D002462:Cell Membrane / Q000378:metabolism*; D002463:Cell Membrane Permeability / Q000502:physiology*; D015696:Gene Products, tat / Q000378:metabolism; D015497:HIV-1 / Q000378:metabolism; D010455:Peptides / Q000378:metabolism*; D054322:tat Gene Products, Human Immunodeficiency Virus
D015696:Gene Products, tat; D010455:Peptides; D054322:tat Gene Products, Human Immunodeficiency Virus; D001120:Arginine