Structural changes in human type I collagen fibrils investigated by force spectroscopy
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Updated: Aug 20, 2026

Preparation of Extracellular Matrix Protein Fibers for Brillouin Spectroscopy
Published on: September 15, 2016
John S Graham1, Anthony N Vomund, Charlotte L Phillips
1Department of Physics and Astronomy, University of Missouri-Columbia, Columbia, MO 65211, USA.
Abstract:
In the field of biomechanics, collagen fibrils are believed to be robust mechanical structures characterized by a low extensibility. Until very recently, information on the mechanical properties of collagen fibrils could only be derived from ensemble measurements performed on complete tissues such as bone, skin, and tendon. Here, we measure force-elongation/relaxation profiles of single collagen fibrils using atomic force microscopy (AFM)-based force spectroscopy (FS). The elongation profiles show that in vitro-assembled human type I collagen fibrils are characterized by a large extensibility. Numerous discontinuities and a plateau in the force profile indicate major reorganization occurring within the fibrils in the 1.5- to 4.5-nN range. Our study demonstrates that newly assembled collagen fibrils are robust structures with a significant reserve of elasticity that could play a determinant role in the extracellular matrix (ECM) remodeling associated with tissue growth and morphogenesis.
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