title: Fibril-mediated oligomerization of pilin-derived protein nanotubes.
abstract: BACKGROUND
  Self-assembling protein nanotubes (PNTs) are an intriguing alternative to carbon nanotubes for applications in bionanotechnology, in part due to greater inherent biocompatibility. The type IV pilus of the gram negative bacteria Pseudomonas aeruginosa is a protein-based fibre composed of a single subunit, the type IV pilin. Engineered pilin monomers from P. aeruginosa strain K122-4 (ΔK122) have been shown to oligomerize into PNTs both in solution and at surfaces. In order to fully exploit PNTs in bionanotechonological settings, an in-depth understanding of their assembly, physical characteristics and robustness, both in solution and when constrained to surfaces, is required.
  
  
  RESULTS
  This study details the effectiveness of multiple initiators of ΔK122-derived PNT oligomerization and characterize the formation of PNTs in solution. The optimal initiator for the oligomerization of ΔK122 in solution was observed to be 2-methyl-2,4-pentanediol (MPD). Conversely, larger PEG molecules do not trigger oligomerization. Multi-angle light scattering analysis indicates that the pilin protein exists in a monomer-dimer equilibrium in solution, and that an intermediate species forms within three hours that then coalesces over time into high molecular weight PNTs. Transmission Electron Microscopic analysis was used to observe the formation of oligomerized ΔK122 fibrils prior to assembly into full-length PNTs.
  
  
  CONCLUSIONS
  The oligomerization of ΔK122 pilin derived PNTs is a fibril mediated process. The optimal trigger for PNT oligomerization in solution is MPD, and the observation that PEGs do not induce oligomerization may enable the oligomerization of pilin-derived PNTs on PEG-functionalized surfaces for implantable bionanodevices.
authors.affiliation: Department of Chemistry, York University, Toronto, ON M3J1P3, Canada.
authors.forename: Anna
authors.initials: A
authors.lastname: Petrov
authors.forename: Stephanie
authors.initials: S
authors.lastname: Lombardo
authors.forename: Gerald F
authors.initials: GF
authors.lastname: Audette
mesh_terms: D002850:Chromatography, Gel; D036781:Fimbriae Proteins / Q000737:chemistry* / Q000378:metabolism*; D010861:Fimbriae, Bacterial / Q000378:metabolism*; D057927:Hydrophobic and Hydrophilic Interactions; D008954:Models, Biological; D043942:Nanotubes / Q000737:chemistry* / Q000648:ultrastructure; D020836:Protein Structure, Quaternary; D011550:Pseudomonas aeruginosa; D012542:Scattering, Radiation; D012996:Solutions; D013997:Time Factors
chemical_list: D012996:Solutions; D036781:Fimbriae Proteins