論文

査読有り
2012年

Binding of Tat peptides on DOPC and DOPG lipid bilayer membrane studied by molecular dynamics simulations

MOLECULAR SIMULATION
  • Shuhei Kawamoto
  • ,
  • Masako Takasu
  • ,
  • Takeshi Miyakawa
  • ,
  • Ryota Morikawa
  • ,
  • Tatsuki Oda
  • ,
  • Shiroh Futaki
  • ,
  • Hidemi Nagao

38
5
開始ページ
366
終了ページ
368
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1080/08927022.2010.536546
出版者・発行元
TAYLOR & FRANCIS LTD

Cell-penetrating peptides (CPPs) have an ability of internalisation to inner cells through plasma membrane. The plasma membrane and lipid bilayer in experiments contain negatively charged lipids. HIV-1 Tat peptide, which is one of the CPPs, has many arginines with positive charge, and strongly interacts with negatively charged lipids. We investigate the difference between neutral lipids, 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), and negatively charged lipids, 1,2-dioleoyl-sn-glycero-3[phospho-rac-(1-glycerol)] (DOPG), by all-atom molecular dynamics simulations. We found that the speed of binding of Tat to lipid membrane for DOPC is more than 10 times faster than the speed for DOPG. The Tat peptides bind to the lipid membrane by attractive interaction between arginine in Tat and phosphates in lipids. Comparing the number of phosphates binding to arginine, DOPG gives a larger number than DOPC. The differences indicate the importance of negatively charged lipids for the investigation of the property of CPPs.

リンク情報
DOI
https://doi.org/10.1080/08927022.2010.536546
J-GLOBAL
https://jglobal.jst.go.jp/detail?JGLOBAL_ID=201502893161571532
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000301953100005&DestApp=WOS_CPL
ID情報
  • DOI : 10.1080/08927022.2010.536546
  • ISSN : 0892-7022
  • eISSN : 1029-0435
  • J-Global ID : 201502893161571532
  • Web of Science ID : WOS:000301953100005

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