Collagen fibrils: nanoscale ropes.
The formation of collagen fibrils from staggered repeats of individual molecules has become "accepted" wisdom. However, for over thirty years now, such a model has failed to resolve several structural and functional questions. In a novel approach, it was found, using atomic force microscopy, that tendon collagen fibrils are composed of subcomponents in a spiral disposition-that is, their structure is similar to that of macroscale ropes. Consequently, this arrangement was modeled and confirmed using elastic rod theory. This work provides new insight into collagen fibril structure and will have wide application-from the design of scaffolds for tissue engineering and a better understanding of pathogenesis of diseases of bone and tendon, to the conservation of irreplaceable parchment-based museum exhibits.
Bozec
Laurent
L
Bone and Mineral Centre, Department of Medicine, and Department of Civil and Environmental Engineering, University College London, London, England. lbozec@ucl.ac.uk
van der Heijden
Gert
G
Horton
Michael
M
D000818:Animals; D001703:Biophysics / Q000379:methods*; D002417:Cattle; D003094:Collagen / Q000737:chemistry*; D003238:Connective Tissue / Q000378:metabolism; D004548:Elasticity; D024022:Fibrillar Collagens / Q000737:chemistry; D018625:Microscopy, Atomic Force; D008958:Models, Molecular; D015233:Models, Statistical; D036103:Nanotechnology / Q000379:methods*; D013710:Tendons / Q000378:metabolism
D024022:Fibrillar Collagens; D003094:Collagen