Nanointerfacial strength between non-collagenous protein and collagen fibrils in antler bone

Antler bone displays considerable toughness through the use of a complex nanofibrous structure of mineralized collagen fibrils (MCFs) bound together by non-collagenous proteins (NCPs). While the NCP regions represent a small volume fraction relative to the MCFs, significant surface area is evolved u...

Full description

Saved in:
Bibliographic Details
Published in:Journal of the Royal Society interface 2014-03, Vol.11 (92), p.20130993-20130993
Main Authors: Hang, Fei, Gupta, Himadri S., Barber, Asa H.
Format: Article
Language:English
Subjects:
Animals
Antlers - chemistry
Antlers - physiology
Biomechanical Phenomena
Bone
Collagen - analysis
Collagen - ultrastructure
Deer
Microscopy, Atomic Force
Microscopy, Electron, Scanning
Nanomechanics
Proteins - analysis
Proteins - ultrastructure
Toughness
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Antler bone displays considerable toughness through the use of a complex nanofibrous structure of mineralized collagen fibrils (MCFs) bound together by non-collagenous proteins (NCPs). While the NCP regions represent a small volume fraction relative to the MCFs, significant surface area is evolved upon failure of the nanointerfaces formed at NCP–collagen fibril boundaries. The mechanical properties of nanointerfaces between the MCFs are investigated directly in this work using an in situ atomic force microscopy technique to pull out individual fibrils from the NCP. Results show that the NCP–fibril interfaces in antler bone are weak, which highlights the propensity for interface failure at the nanoscale in antler bone and extensive fibril pullout observed at antler fracture surfaces. The adhesion between fibrils and NCP is additionally suggested as being rate dependent, with increasing interfacial strength and fracture energy observed when pullout velocity decreases.
ISSN:1742-5689
1742-5662
DOI:10.1098/rsif.2013.0993