Bioengineered flagella protein nanotubes with cysteine loops: self-assembly and manipulation in an optical trap.
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.
Kumara
Mudalige Thilak
MT
Department of Chemistry and Nanotechnology Research and Computation Center, Western Michigan University, Kalamazoo, Michigan 49008-5410, USA.
Srividya
Narayanan
N
Muralidharan
Subra
S
Tripp
Brian C
BC
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
D046912:Multiprotein Complexes; D005408:Flagellin