Membrane-permeable arginine-rich peptides and the translocation mechanisms.
The intracellular delivery of proteins and other bioactive molecules using membrane-permeable carrier peptide vectors opens the possibility of establishing novel methods of elucidating and controlling cell functions with therapeutic potentials. One of the most typical peptide vectors is a short, arginine-rich peptide segment derived from the human immunodeficiency virus (HIV)-1 Tat protein. We have shown that not only the Tat peptide, but also various arginine-rich oligopeptides possess very similar characteristics in translocation and abilities as a delivery vector. This review summarizes the structures of these peptide vectors, especially the Tat and other arginine-rich peptides, and the current understanding of their internalization mechanisms.
Futaki
Shiroh
S
Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan; PRESTO, Japan Science and Technology Corporation (JST), Kawaguchi, Saitama 332-0012, Japan. futaki@scl.kyoto-u.ac.jp
D000818:Animals; D001120:Arginine / Q000031:analogs & derivatives / Q000378:metabolism; D001692:Biological Transport / Q000502:physiology; D002352:Carrier Proteins / Q000378:metabolism / Q000502:physiology*; D002463:Cell Membrane Permeability / Q000502:physiology*; D057846:Cell-Penetrating Peptides; D015696:Gene Products, tat / Q000378:metabolism*; D015497:HIV-1; D006801:Humans; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D013329:Structure-Activity Relationship; D054322:tat Gene Products, Human Immunodeficiency Virus
D002352:Carrier Proteins; D057846:Cell-Penetrating Peptides; D015696:Gene Products, tat; D010455:Peptides; D054322:tat Gene Products, Human Immunodeficiency Virus; D001120:Arginine; C414409:penetratin