2003年9月
Membrane permeability commonly shared among arginine-rich peptides
JOURNAL OF MOLECULAR RECOGNITION
- ,
- ,
- 巻
- 16
- 号
- 5
- 開始ページ
- 260
- 終了ページ
- 264
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1002/jmr.635
- 出版者・発行元
- JOHN WILEY & SONS LTD
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 (C) 2003 John Wiley Sons, Ltd.
- リンク情報
- ID情報
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- DOI : 10.1002/jmr.635
- ISSN : 0952-3499
- PubMed ID : 14523938
- Web of Science ID : WOS:000185822100007