Short peptide motifs for long-lasting anchoring to the cell surface

Masayoshi Matsuda, Wataru Hatanaka, Masafumi Takeo, Chan Woo Kim, Takuro Niidome, Tatsuhiro Yamamoto, Akihiro Kishimura, Takeshi Mori, Yoshiki Katayama

研究成果: ジャーナルへの寄稿記事

18 引用 (Scopus)

抄録

A rational design strategy has been developed for the construction of stable peptide-based anchors for the efficient modification of cell surfaces. Six types of peptide composed of five residues with divalent hydrophobic groups have been designed using this new strategy. Among them, a peptide with a sequence of NBD-Lys-Lys(X)-Lys-Lys-Lys(X)-NH2 (NBD: fluorophore, Lys(X): N-ε-palmitoyl-L-lysine) was found to show the highest modification efficacy and longevity in culture medium. The good performance of this peptide was attributed to (1) its high aqueous solubility, which allowed it to partition from the medium to the cell surface, and (2) the high binding affinity of the saturated palmitoyl groups to the cell membrane. We found that the distribution of the peptide was affected by recycling endosome, which enabled the representation of the peptide following its endocytotic disappearance from the cell membrane. Biotin was also presented on the cell surface using this peptide-based anchor to examine its recognition by streptavidin. The efficacy of the recognition process increased as the length of the oligoethylene glycol spacer increased, indicating that it was necessary for the biotin tag to move away from the membrane glycoproteins on the cell surface to facilitate its efficient recognition by streptavidin. (Figure Presented).

元の言語英語
ページ(範囲)2134-2143
ページ数10
ジャーナルBioconjugate Chemistry
25
発行部数12
DOI
出版物ステータス出版済み - 12 17 2014

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Peptides
Streptavidin
Cell membranes
Biotin
Anchors
lysyllysine
Cell Membrane
Glycoproteins
Glycols
Fluorophores
Endosomes
Membrane Glycoproteins
Solubility
Lysine
Culture Media
Recycling
Membranes

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Biomedical Engineering
  • Pharmacology
  • Pharmaceutical Science
  • Organic Chemistry

これを引用

Matsuda, M., Hatanaka, W., Takeo, M., Kim, C. W., Niidome, T., Yamamoto, T., ... Katayama, Y. (2014). Short peptide motifs for long-lasting anchoring to the cell surface. Bioconjugate Chemistry, 25(12), 2134-2143. https://doi.org/10.1021/bc500465j

Short peptide motifs for long-lasting anchoring to the cell surface. / Matsuda, Masayoshi; Hatanaka, Wataru; Takeo, Masafumi; Kim, Chan Woo; Niidome, Takuro; Yamamoto, Tatsuhiro; Kishimura, Akihiro; Mori, Takeshi; Katayama, Yoshiki.

:: Bioconjugate Chemistry, 巻 25, 番号 12, 17.12.2014, p. 2134-2143.

研究成果: ジャーナルへの寄稿記事

Matsuda, M, Hatanaka, W, Takeo, M, Kim, CW, Niidome, T, Yamamoto, T, Kishimura, A, Mori, T & Katayama, Y 2014, 'Short peptide motifs for long-lasting anchoring to the cell surface', Bioconjugate Chemistry, 巻. 25, 番号 12, pp. 2134-2143. https://doi.org/10.1021/bc500465j
Matsuda M, Hatanaka W, Takeo M, Kim CW, Niidome T, Yamamoto T その他. Short peptide motifs for long-lasting anchoring to the cell surface. Bioconjugate Chemistry. 2014 12 17;25(12):2134-2143. https://doi.org/10.1021/bc500465j
Matsuda, Masayoshi ; Hatanaka, Wataru ; Takeo, Masafumi ; Kim, Chan Woo ; Niidome, Takuro ; Yamamoto, Tatsuhiro ; Kishimura, Akihiro ; Mori, Takeshi ; Katayama, Yoshiki. / Short peptide motifs for long-lasting anchoring to the cell surface. :: Bioconjugate Chemistry. 2014 ; 巻 25, 番号 12. pp. 2134-2143.
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