Mechanical response of individual collagen fibrils in loaded tendon as measured by atomic force microscopy

Rigozzi, S.; Stemmer, Andreas; Müller, Ralph; Snedeker, Jess G.

doi:10.1016/j.jsb.2011.07.002

Cited by 51 publications

(54 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…From this perspective, otherwise physiological loads in aged tendons could involve fiber "over-stretching" that leads to accelerated accumulation of damage. How fibril level response relates to collagen fiber mechanics and damage accumulation remains to be investigated using sub-microscopic imaging approaches such as atomic force microscopy (Rigozzi et al, 2011) or X-ray scattering techniques (Gupta et al, 2010).…”

Section: Discussionmentioning

confidence: 99%

Advanced glycation end-products diminish tendon collagen fiber sliding

et al. 2013

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 99%

Advanced glycation end-products diminish tendon collagen fiber sliding

et al. 2013

View full text Add to dashboard Cite

“…The covalent crosslinks between collagen molecules and microfibrils plays an important role in stabilizing the fibrils and the collagen network. Rigozzi et al [22] employed an atomic force microscope to characterize the diameter and periodic banding (D-period) of individual collagen fibrils under macroscopic tendon extension. The D-period banding and fibril diameter were statistically unchanged for tendon strain of 5%.…”

Section: Discussionmentioning

confidence: 99%

An Experimental and Modeling Study of the Viscoelastic Behavior of Collagen Gel

Xu¹,

Zhang

2013

Journal of Biomechanical Engineering

View full text Add to dashboard Cite

The macroscopic viscoelastic behavior of collagen gel was studied through relaxation time distribution spectrum obtained from stress relaxation tests and viscoelastic constitutive modeling. Biaxial stress relaxation tests were performed to characterize the viscoelastic behavior of collagen gel crosslinked with Genipin solution. Relaxation time distribution spectrum was obtained from the stress relaxation data by inverse Laplace transform. Peaks at the short (0.3 s-1 s), medium (3 s-90 s), and long relaxation time (>200 s) were observed in the continuous spectrum, which likely correspond to relaxation mechanisms involve fiber, interfibril, and fibril sliding. The intensity of the long-term peaks increases with higher initial stress levels indicating the engagement of collagen fibrils at higher levels of tissue strain. We have shown that the stress relaxation behavior can be well simulated using a viscoelastic model with viscous material parameters obtained directly from the relaxation time spectrum. Results from the current study suggest that the relaxation time distribution spectrum is useful in connecting the macro-level viscoelastic behavior of collagen matrices with micro-level structure changes.

show abstract

“…It is at the level of the fiber where biologically relevant cell-level mechanical stimuli emerge, since the fiber comprises the structural unit with which tendon cells directly interact. Finally, the properties of the individual collagen fibrils (submicron-scale) that comprise the collagen fiber (cell-scale) are increasingly well described [87][88][89][90]. These supramolecular collagen structures range in diameter from tens to hundreds of nanometers, with lengths that can span centimeters [91].…”

Section: Tendon Core -Multiscale Structure and Functionmentioning

confidence: 99%