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 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.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Amino Acid Sequence
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Amino Acids, Branched-Chain / chemistry
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Amino Acids, Branched-Chain / metabolism
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Animals
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Arginine / chemistry*
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Arginine / metabolism*
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Cell Membrane Permeability*
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Gene Products, rev / chemical synthesis
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Gene Products, rev / chemistry
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Gene Products, rev / metabolism
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Gene Products, tat / chemistry
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Gene Products, tat / metabolism
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HIV-1 / chemistry
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HIV-1 / metabolism
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HeLa Cells
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Humans
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Peptide Fragments / chemistry
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Peptide Fragments / metabolism
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Peptides / chemical synthesis
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Peptides / chemistry*
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Peptides / classification
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Peptides / metabolism*
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Protein Transport*
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Structure-Activity Relationship
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rev Gene Products, Human Immunodeficiency Virus
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tat Gene Products, Human Immunodeficiency Virus
Substances
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Amino Acids, Branched-Chain
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Gene Products, rev
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Gene Products, tat
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Peptide Fragments
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Peptides
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rev Gene Products, Human Immunodeficiency Virus
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tat Gene Products, Human Immunodeficiency Virus
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tat peptide (48-60), Human immunodeficiency virus 1
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Arginine