Membrane permeability commonly shared among arginine‐rich peptides

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Abstract
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. Copyright © 2003 John Wiley & Sons, Ltd.