論文

査読有り
2014年11月1日

Charge-Separated Fmoc-peptide β-Sheets: Sequence-Secondary Structure Relationship for Arranging Charged Side Chains on Both Sides

ASIAN JOURNAL OF ORGANIC CHEMISTRY
  • Nakayama,Toru
  • ,
  • Sakuraba,Taro
  • ,
  • Tomita,Shunsuke
  • ,
  • Kaneko,Akira
  • ,
  • Takai,Eisuke
  • ,
  • Shiraki,Kentaro
  • ,
  • Tashiro,Kentaro
  • ,
  • Ishii,Noriyuki
  • ,
  • Hasegawa,Yuri
  • ,
  • Yamada,Yoichi
  • ,
  • Kumai,Reiji
  • ,
  • Yamamoto,Yohei

3
11
開始ページ
1182
終了ページ
1188
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1002/ajoc.201402129
出版者・発行元
WILEY-V C H VERLAG GMBH

beta-Sheet formation from fluorenylmethoxycarbonyl (Fmoc)-substituted polar oligopeptides was demonstrated, where acidic and basic side chains are located separately on either side of the beta-sheet surfaces. For yielding such charge-separated beta-sheets, self-assembly of 18 pentapeptides was studied, all of which contain glutamic acid (E), lysine (K), and valine (V). Fmoc-pentapeptides containing one E and one K all formed fibrillar nano-structures consisting of stacked beta-sheets. On the other hand, Fmoc-pentapeptides containing two E and two K formed beta-sheet fibrils only when V was located at the center and separated two EK pairs. Photoluminescence studies of these peptides in a glycine buffer containing thioflavin T revealed a clear relationship between the amino acid sequence and secondary structure, where the location of neutral V plays a pivotal role for the bsheet formation. The beta-sheet formation propensity was further supported by computer simulation studies with the TANGO algorithm.

リンク情報
DOI
https://doi.org/10.1002/ajoc.201402129
Scopus
https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85027928571&origin=inward
Scopus Citedby
https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=85027928571&origin=inward

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