title: Mechanical properties of collagen fibrils.
abstract: The formation of collagen fibers from staggered subfibrils still lacks a universally accepted model. Determining the mechanical properties of single collagen fibrils (diameter 50-200 nm) provides new insights into collagen structure. In this work, the reduced modulus of collagen was measured by nanoindentation using atomic force microscopy. For individual type 1 collagen fibrils from rat tail, the modulus was found to be in the range from 5 GPa to 11.5 GPa (in air and at room temperature). The hypothesis that collagen anisotropy is due to the subfibrils being aligned along the fibril axis is supported by nonuniform surface imprints performed by high load nanoindentation.
authors.affiliation: Bone and Mineral Centre, Department of Medicine, London Centre for Nanotechnology, University College London, London, United Kingdom.
authors.forename: Marco P E
authors.initials: MP
authors.lastname: Wenger
authors.forename: Laurent
authors.initials: L
authors.lastname: Bozec
authors.forename: Michael A
authors.initials: MA
authors.lastname: Horton
authors.forename: Patrick
authors.initials: P
authors.lastname: Mesquida
mesh_terms: D000818:Animals; D016880:Anisotropy; D001696:Biomechanical Phenomena; D024042:Collagen Type I / Q000737:chemistry* / Q000648:ultrastructure; D018625:Microscopy, Atomic Force; D008962:Models, Theoretical; D051381:Rats; D014867:Water / Q000737:chemistry
chemical_list: D024042:Collagen Type I; D014867:Water