Cross-link stabilization does not affect the response of collagen molecules, fibrils, or tendons to tensile overload.

We investigated whether immature allysine-derived cross-links provide mechanically labile linkages by exploring the effects of immature cross-link stabilization at three levels of collagen hierarchy: damaged fibril morphology, whole tendon mechanics, and molecular stability. Tendons from the tails of young adult steers were either treated with sodium borohydride (NaBH₄) to stabilize labile cross-links, exposed only to the buffer used during stabilization treatment, or maintained as untreated controls. One-half of each tendon was then subjected to five cycles of subrupture overload. Morphologic changes to collagen fibrils resulting from overload were investigated using scanning electron microscopy, and changes in the hydrothermal stability of collagen molecules were assessed using hydrothermal isometric tension testing. NaBH4 cross-link stabilization did not affect the response of tendon collagen to tensile overload at any of the three levels of hierarchy studied. Cross-link stabilization did not prevent the characteristic overload-induced mode of fibril damage that we term discrete plasticity. Similarly, stabilization did not alter the mechanical response of whole tendons to overload, and did not prevent an overload-induced thermal destabilization of collagen molecules. Our results indicate that hydrothermally labile cross-links may not be as mechanically labile as was previously thought.