Combining tensile testing and structural analysis at the single collagen fibril level

Andrew S. Quigley, Stéphane Bancelin, Dylan Deska-Gauthier, François Légaré, Samuel P. Veres, Laurent Kreplak
Sci Data. 2018-10-23; 5(1):
DOI: 10.1038/sdata.2018.229

PubMed
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Tensile testing to failure followed by imaging is a simple way of studying the
structure-function relationship of connective tissues such as skin, tendon, and
ligament. However, interpretation of these datasets is complex due to the
hierarchical structures of the tissues spanning six or more orders of magnitude
in length scale. Here we present a dataset obtained through the same scheme at
the single collagen fibril level, the fundamental tensile element of load-bearing
tissues. Tensile testing was performed on fibrils extracted from two types of
bovine tendons, adsorbed on a glass surface and glued at both ends. An atomic
force microscope (AFM) was used to pull fibrils to failure in bowstring geometry.
The broken fibrils were then imaged by AFM for morphological characterization, by
second harmonic generation microscopy to assess changes to molecular packing, and
by fluorescence microscopy after incubation with a peptide probe that binds
specifically to denatured collagen molecules. This dataset linking stress-strain
curves to post-failure molecular changes is useful for researchers modelling or
designing functional protein materials.

 

Auteurs Bordeaux Neurocampus