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, Ehud Gazit*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

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.

Original languageAmerican English
Article number13482
JournalNature Communications
Volume7
DOIs
StatePublished - 17 Nov 2016

Bibliographical note

Publisher Copyright:
© 2016 The Author(s).

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