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


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 ?-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.

SUBMITTER: Guterman T 

PROVIDER: S-EPMC5473601 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature

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

Guterman Tom T   Kornreich Micha M   Stern Avigail A   Adler-Abramovich Lihi L   Porath Danny D   Beck Roy R   Shimon Linda J W LJW   Gazit Ehud E  

Nature communications 20161117


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 s  ...[more]

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