title: Structural and mechanical study of a self-assembling protein nanotube.
abstract: We report a structural characterization of self-assembling nanostructures. Using atomic force microscopy (AFM), we discovered that partially hydrolyzed alpha-lactalbumin organizes in a 10-start helix forming tubes with diameters of only 21 nm. We probed the mechanical strength of these nanotubes by locally indenting them with an AFM tip. To extract the material properties of the nanotubes, we modeled the experiment using finite element methods. Our study shows that artificial helical protein self-assembly can yield very stable, strong structures that can function either as a model system for artificial self-assembly or as a nanostructure with potential for practical applications.
authors.affiliation: NIZO food research, P.O. Box 20, 6710 BA Ede, The Netherlands. joanke@mit.edu
authors.forename: J F
authors.initials: JF
authors.lastname: Graveland-Bikker
authors.forename: I A T
authors.initials: IA
authors.lastname: Schaap
authors.forename: C F
authors.initials: CF
authors.lastname: Schmidt
authors.forename: C G
authors.initials: CG
authors.lastname: de Kruif
mesh_terms: D003198:Computer Simulation; D003460:Crystallization / Q000379:methods*; D019281:Dimerization; D004548:Elasticity; D007768:Lactalbumin / Q000737:chemistry* / Q000648:ultrastructure*; D008422:Materials Testing; D019563:Mechanics; D008956:Models, Chemical; D046912:Multiprotein Complexes / Q000737:chemistry / Q000648:ultrastructure; D036103:Nanotechnology / Q000379:methods; D043942:Nanotubes / Q000737:chemistry* / Q000648:ultrastructure*; D010316:Particle Size; D011485:Protein Binding; D011487:Protein Conformation; D013314:Stress, Mechanical; D013718:Tensile Strength
chemical_list: D046912:Multiprotein Complexes; D007768:Lactalbumin