A self-assembled protein nanotube with high aspect ratio.
Production of a self-assembled protein nanotube achieved through engineering of the 11mer ring protein trp RNA-binding attenuation protein is described. The produced mutant protein is able to stack in solution to produce an extremely narrow, uniform nanotube apparently stabilized by a mixture of disulfide bonds and hydrophobic interactions. Assembly is reversible and the length of tube can potentially be controlled. Large quantities of hollow tubes 8.5 nm in overall diameter with lengths varying from 7 nm to over 1 microm are produced. The structure is analyzed using transmission electron microscopy, atomic force microscopy, mass spectrometry, and single-particle analysis and it is found that component rings stack in a head-to-head fashion. The internal diameter of the tube is 2.5 nm, and the amino acid residues lining the central cavity can be mutated, raising the possibility that the tube can be filled with a variety of conducting or semiconducting materials.
Miranda
Frederico F
FF
Protein Design Laboratory, Yokohama City University, Suehiro-cho, Tsurumi-ku, Japan.
Iwasaki
Kenji
K
Akashi
Satoko
S
Sumitomo
Koji
K
Kobayashi
Mime
M
Yamashita
Ichiro
I
Tame
Jeremy R H
JR
Heddle
Jonathan G
JG
D004591:Electrophoresis, Polyacrylamide Gel; D018625:Microscopy, Atomic Force; D046529:Microscopy, Electron, Transmission; D043942:Nanotubes; D011506:Proteins / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D011506:Proteins