Microstructural characterization of vocal folds toward a strain-energy model of collagen remodeling

Amir K. Miri, Hossein K. Heris, Umakanta Tripathy, Paul W. Wiseman, Luc Mongeau

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


Collagen fibrils are believed to control the immediate deformation of soft tissues under mechanical load. Most extracellular matrix proteins remain intact during frozen sectioning, which allows them to be scanned using atomic force microscopy (AFM). Collagen fibrils are distinguishable because of their periodic roughness wavelength. In the present study, the shape and organization of collagen fibrils in dissected porcine vocal folds were quantified using nonlinear laser scanning microscopy data at the micrometer scale and AFM data at the nanometer scale. Rope-shaped collagen fibrils were observed. The geometric characteristics for the fibrils were fed into a hyperelastic model to predict the biomechanical response of the tissue. The model simulates the micrometer-scale unlocking behavior of collagen bundles when extended from their unloaded configuration. Force spectroscopy using AFM was used to estimate the stiffness of collagen fibrils (1 ± 0.5 MPa). The presence of rope-shaped fibrils is postulated to change the slope of the force-deflection response near the onset of nonlinearity. The proposed model could ultimately be used to evaluate changes in elasticity of soft tissues that result from the collagen remodeling.

Original languageEnglish (US)
Pages (from-to)7957-7967
Number of pages11
JournalActa Biomaterialia
Issue number8
StatePublished - Aug 2013
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Biomaterials
  • Biochemistry
  • Biomedical Engineering
  • Molecular Biology


  • Atomic force microscopy
  • Collagen
  • Helix
  • Nonlinear laser scanning microscopy
  • Strain energy function


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