論文

査読有り
2017年6月

Tuning the Viscoelasticity of Peptide Vesicles by Adjusting Hydrophobic Helical Blocks Comprising Amphiphilic Polypeptides

LANGMUIR
  • Cheol Joo Kim
  • ,
  • Motoki Ueda
  • ,
  • Tomoya Imai
  • ,
  • Junji Sugiyama
  • ,
  • Shunsaku Kimura

33
22
開始ページ
5423
終了ページ
5429
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1021/acs.langmuir.7b00289
出版者・発行元
AMER CHEMICAL SOC

Amphiphilic block polypeptides of
[GRAPHIC]
poly(sarcosine)-b-(L-Val-Aib)(6) and poly(sarcosine)-b-(L-Leu-Aib)(6) and their steteoisomers were self-assembled in water. Three kinds of binary systems of poly(sarcosine)-b-(L-Leu-Aib)(6) with poly(sarcosine)-b-poly(D-Leu-Aib)(6), poly(sarcosine)-b-poly(L-Val-Aib)(6), or poly(sarcosine)-b-(D-Val-Aib)(6) generated vesicles of 200 nm diameter. The viscoelasticity of the vesicle membranes was evaluated by the nanoindentation method using AFM in water. The elasticity of the poly(sarcosine)-b-(L-Leu-Aib)(6)/poly(sarcosine)-b-poly(D-Leu-Aib)(6) vesicle was 11 fold higher than that of the egg yolk liposome but decreased in coinbinations,of the Leu- and Val-based amphiphilic polypeptides. The membrane elasticity is found to be adjustable by a suitable combination of helical brocks in terms of stereocomplex formation and the interdigitation of side chains among helices in the molecular assemblies.

リンク情報
DOI
https://doi.org/10.1021/acs.langmuir.7b00289
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000403035200011&DestApp=WOS_CPL
ID情報
  • DOI : 10.1021/acs.langmuir.7b00289
  • ISSN : 0743-7463
  • Web of Science ID : WOS:000403035200011

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