論文

査読有り
2011年2月

Rational design of peptide nanotubes for varying diameters and lengths

JOURNAL OF PEPTIDE SCIENCE
  • Motoki Ueda
  • ,
  • Akira Makino
  • ,
  • Tomoya Imai
  • ,
  • Junji Sugiyama
  • ,
  • Shunsaku Kimura

17
2
開始ページ
94
終了ページ
99
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1002/psc.1304
出版者・発行元
JOHN WILEY & SONS LTD

Amphiphilic helical peptides (Sar)(m)-b-(L-Leu-Aib)(n) (m = 22-25; n = 7, 8, 10) with a hydrophobic block as a right-handed helix were synthesized and their mixtures with (Sar)(25)-b-(D-Leu-Aib)(6) containing the hydrophobic block as a left-handed helix were examined in their molecular assembly formation. The single component (Sar)(25)-b-(D-Leu-Aib)(6) forms peptide nanotubes of 70 nm diameter and 200 nm length. The two-component mixtures of (Sar)(25)-b-(D-Leu-Aib)(6) with (Sar)(24)-b-(L-Leu-Aib)(7), (Sar)(22)-b-(L-Leu-Aib)(8), and (Sar)(25)-b-(L-Leu-Aib)(1)0 yield peptide nanotubes of varying dimensions with 200 nm diameter and 400 nm length, 70 nm diameter and several micrometer length (maximum 30 mu m), and 70 nm diameter and 100-600 nm length, respectively. The right-handed and the left-handed helix were thus found to be molecularly mixed due to the stereo-complex formation and to generate nanotubes of different sizes. When the mismatch of the hydrophobic helical length between the two components was of four residues, the longest nanotube was generated. Correspondingly, the hydrophobic helical segments have to interdigitate with an anti-parallel orientation at the hydrophobic core region of the nanotube. Copyright (C) 2010 European Peptide Society and John Wiley & Sons, Ltd.

リンク情報
DOI
https://doi.org/10.1002/psc.1304
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000287164000004&DestApp=WOS_CPL
ID情報
  • DOI : 10.1002/psc.1304
  • ISSN : 1075-2617
  • Web of Science ID : WOS:000287164000004

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