title: Self-assembled peptide nanotubes are uniquely rigid bioinspired supramolecular structures.
abstract: We recently presented a novel class of self-assembled diphenylalanine-based peptide nanotubes. Here, for the first time, we present their mechanical properties, which we directly measured through indentation type experiments using atomic force microscopy. We find that the averaged point stiffness of the nanotubes is 160 N/m, and that they have a correspondingly high Young's modulus of approximately 19 GPa, as calculated by finite element analysis. This high value places these peptide nanotubes among the stiffest biological materials presently known, making them attractive building blocks for the design and assembly of biocompatible nanodevices.
authors.affiliation: Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel.
authors.forename: Nitzan
authors.initials: N
authors.lastname: Kol
authors.forename: Lihi
authors.initials: L
authors.lastname: Adler-Abramovich
authors.forename: David
authors.initials: D
authors.lastname: Barlam
authors.forename: Roni Z
authors.initials: RZ
authors.lastname: Shneck
authors.forename: Ehud
authors.initials: E
authors.lastname: Gazit
authors.forename: Itay
authors.initials: I
authors.lastname: Rousso
mesh_terms: D003460:Crystallization / Q000379:methods*; D019281:Dimerization; D004548:Elasticity; D008422:Materials Testing; D008956:Models, Chemical; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000032:analysis / Q000737:chemistry / Q000648:ultrastructure; D043942:Nanotubes / Q000032:analysis / Q000737:chemistry* / Q000648:ultrastructure*; D010316:Particle Size; D010455:Peptides / Q000032:analysis / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D013314:Stress, Mechanical
chemical_list: D046912:Multiprotein Complexes; D010455:Peptides