MISC

2007年8月

Creation of a novel cell penetrating peptide, using a random 18mer peptides library

Pharmazie
  • T. Nomura
  • M. Kawamura
  • H. Shibata
  • Y. Abe
  • A. Ohkawa
  • Y. Mukai
  • T. Sugita
  • S. Imai
  • K. Nagano
  • T. Okamoto
  • Y. Tsutsumi
  • Haruhiko Kamada
  • S. Nakagawa
  • S. Tsunoda
  • 全て表示

62
8
開始ページ
569
終了ページ
573
記述言語
英語
掲載種別
DOI
10.1691/ph.2007.8.6278

Cell penetrating peptides (CPPs) have drawn attention as carriers for intracellular drug delivery. It is commonly believed that TAT peptide is the best carrier among the existing CPPs due to its high translocational activity. Despite considerable research, the cellular uptake mechanism of TAT peptide remains unclear. Additionally, the transduction efficiency of TAT peptide is insufficient for use in intracellular therapy. In this study, we attempted to identify novel CPPs from a random 18mer peptide library using a phage display system. To isolate novel CPPs more effectively, PSIF (protein synthesis inhibition factor) was used with the screening system. Consequently, we isolated 7 novel CPPs from the library and determined by flow cytometry and confocal laser microscopy that these CPPs were taken up into cells. Once the cellular uptake pathway of these CPPs has been determined, it may be possible to use them for intracellular therapy.

リンク情報
DOI
https://doi.org/10.1691/ph.2007.8.6278
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/17867548
ID情報
  • DOI : 10.1691/ph.2007.8.6278
  • ISSN : 0031-7144
  • PubMed ID : 17867548
  • SCOPUS ID : 34548281694

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