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Formation of bacterial pilus-like nanofibres by designed minimalistic self-assembling peptides

Author

Listed:
  • Tom Guterman

    (George S. Wise Faculty of Life Sciences, Tel Aviv University)

  • Micha Kornreich

    (The Raymond and Beverly Sackler School of Physics and Astronomy, Tel Aviv University)

  • Avigail Stern

    (Institute of Chemistry and The Center for Nanoscience and Nanotechnology, The Hebrew University of Jerusalem, Edmond J. Safra Campus)

  • Lihi Adler-Abramovich

    (The Goldschleger School of Dental Medicine, Sackler Faculty of Medicine, Tel Aviv University)

  • Danny Porath

    (Institute of Chemistry and The Center for Nanoscience and Nanotechnology, The Hebrew University of Jerusalem, Edmond J. Safra Campus)

  • Roy Beck

    (The Raymond and Beverly Sackler School of Physics and Astronomy, Tel Aviv University)

  • Linda J. W. Shimon

    (Weizmann Institute of Science)

  • Ehud Gazit

    (George S. Wise Faculty of Life Sciences, Tel Aviv University
    Iby and Aladar Fleischman Faculty of Engineering, Tel Aviv University)

Abstract

Mimicking the multifunctional bacterial type IV pili (T4Ps) nanofibres provides an important avenue towards the development of new functional nanostructured biomaterials. Yet, the development of T4Ps-based applications is limited by the inability to form these nanofibres in vitro from their pilin monomers. Here, to overcome this limitation, we followed a reductionist approach and designed a self-assembling pilin-based 20-mer peptide, derived from the presumably bioelectronic pilin of Geobacter sulfurreducens. The designed 20-mer, which spans sequences from both the polymerization domain and the functionality region of the pilin, self-assembled into ordered nanofibres. Investigation of the 20-mer revealed that shorter sequences which correspond to the polymerization domain form a supramolecular β-sheet, contrary to their helical configuration in the native T4P core, due to alternative molecular recognition. In contrast, the sequence derived from the functionality region maintains a native-like, helical conformation. This study presents a new family of self-assembling peptides which form T4P-like nanostructures.

Suggested Citation

  • Tom Guterman & Micha Kornreich & Avigail Stern & Lihi Adler-Abramovich & Danny Porath & Roy Beck & Linda J. W. Shimon & Ehud Gazit, 2016. "Formation of bacterial pilus-like nanofibres by designed minimalistic self-assembling peptides," Nature Communications, Nature, vol. 7(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13482
    DOI: 10.1038/ncomms13482
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    Cited by:

    1. Bin Xue & Zoobia Bashir & Yachong Guo & Wenting Yu & Wenxu Sun & Yiran Li & Yiyang Zhang & Meng Qin & Wei Wang & Yi Cao, 2023. "Strong, tough, rapid-recovery, and fatigue-resistant hydrogels made of picot peptide fibres," Nature Communications, Nature, vol. 14(1), pages 1-10, December.

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