論文

査読有り
2020年1月

Conversion of cationic amphiphilic lytic peptides to cell-penetration peptides

PEPTIDE SCIENCE
  • Hao-Hsin Yu
  • ,
  • Kentarou Sakamoto
  • ,
  • Misao Akishiba
  • ,
  • Naoki Tamemoto
  • ,
  • Hisaaki Hirose
  • ,
  • Ikuhiko Nakase
  • ,
  • Miki Imanishi
  • ,
  • Fatemeh Madani
  • ,
  • Astrid Graslund
  • ,
  • Shiroh Futaki

112
1
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1002/pep2.24144
出版者・発行元
WILEY

Accomplishment of efficient intracellular delivery of bioactive peptides and proteins have been reported via conjugation of peptides having membrane permeation ability (i.e., cell-penetrating peptides [CPPs]), where a physiological uptake system of extracellular materials, endocytosis, often plays a role. When endocytosed, the bioactive peptides and proteins are encapsulated into vesicular compartment named endosomes, and have to escape into the cytosol with the help of tethered CPPs for obtaining the expected bioactivities. Therefore, CPPs having improved endosomolytic activity is necessary. We here introduce an approach to employ hemolytic peptides as a new class of CPPs, which was designed to attenuate their membrane perturbation ability on cell surfaces while recovering the membrane lytic activity under endosomal conditions (i.e., the attenuated cationic amphiphilic lytic [ACAL] peptides). This was realized by introducing negatively charged glutamic acid (Glu) residues into the potential hydrophobic face of the cationic amphiphilic peptides. The applicability of these peptides for CPPs was evaluated through the intracellular delivery of shepherdin, an apoptosis-inducing peptide.

Web of Science ® 被引用回数 : 1

リンク情報
DOI
https://doi.org/10.1002/pep2.24144
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000508926900012&DestApp=WOS_CPL

エクスポート
BibTeX RIS