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

Tom Guterman, Micha Kornreich, Avigail Stern, Lihi Adler-Abramovich, Danny Porath, Roy Beck, Linda J. W. Shimon and Ehud Gazit ()
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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

Nature Communications, 2016, vol. 7, issue 1, 1-10

Abstract: 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.

Date: 2016
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DOI: 10.1038/ncomms13482

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