Abstract
Collagen, the dominating material in the extracellular matrix, provides the strength, elasticity and mechanical stability to the organisms. The mechanical property of collagen is mainly dominated by its surrounding environments. However, the variation and origin of the mechanics of collagen fibril under different concentrations of calcium ions (χCa) remains unknown. By using the atomic force microscopy based nanoindentation, the mechanics and structure of individual type II collagen fibril were first investigated under different χCa in this study. The results demonstrate that both of the mechanical and structural properties of the collagen fibril show a prominent dependence on χCa. The mechanism of χCa-dependence of the collagen fibril was attributed to the chelation between collagen molecules and the calcium ions. Given the role of calcium in the pathology of osteoarthritis, the current study may cast new light on the understanding of osteoarthritis and other soft tissue hardening related diseases in the future.
Highlights
Extensively investigated[7,12,13,14,15]
Using Atomic force microscopy (AFM)-based nanoindentation, we have first investigated the effect of calcium ions on the mechanics and structure of individual type II collagen fibril in this study
It was found that both of structural and mechanical characteristics of the type II collagen fibril are dependent on the concentration of calcium ions
Summary
Extensively investigated[7,12,13,14,15]. how external ions (i.e., calcium ions) affect both structural and mechanical properties of individual collagen fibril is still ambiguous, especially under the nanoscale level. The structural properties (D-band periodicity and the height difference between the gap and overlap regions) of type II collagen fibril were investigated. It was found that the structural and mechanical behaviors of individual type II collagen fibril are significantly depending on the concentration of calcium ions (χCa). When 2 mM
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