title: Bioengineered flagella protein nanotubes with cysteine loops: self-assembly and manipulation in an optical trap.
abstract: An E. coli flagellin protein, termed FliTrx, was investigated for use as a novel form of self-assembling protein nanotube. This protein was genetically engineered to display constrained peptide loops with a series of different thiol, cationic, anionic, and imidazole functional groups. "Cys-loop" thiol variants consisting of 6 and 12 cysteine residues were isolated in the form of disulfide-linked nanotube bundles, a novel nanomaterial. Bundles were characterized by fluorescence microscopy, transmission electron microscopy, and optical trapping.
authors.affiliation: Department of Chemistry and Nanotechnology Research and Computation Center, Western Michigan University, Kalamazoo, Michigan 49008-5410, USA.
authors.forename: Mudalige Thilak
authors.initials: MT
authors.lastname: Kumara
authors.forename: Narayanan
authors.initials: N
authors.lastname: Srividya
authors.forename: Subra
authors.initials: S
authors.lastname: Muralidharan
authors.forename: Brian C
authors.initials: BC
authors.lastname: Tripp
mesh_terms: D004548:Elasticity; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005408:Flagellin / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure*; D008422:Materials Testing; D008846:Micromanipulation / Q000379:methods; D046912:Multiprotein Complexes / Q000737:chemistry / Q000648:ultrastructure; D049329:Nanostructures / Q000737:chemistry* / Q000648:ultrastructure*; D043942:Nanotubes / Q000737:chemistry* / Q000648:ultrastructure*; D055095:Optics and Photonics; D011487:Protein Conformation; D015202:Protein Engineering / Q000379:methods*; D013314:Stress, Mechanical
chemical_list: D046912:Multiprotein Complexes; D005408:Flagellin