Dual scale biomechanics of extracellular matrix proteins probed by Brillouin scattering and quasistatic tensile testing
Society of Photo-optical Instrumentation Engineers (SPIE)
Copyright © 2018 Society of Photo-Optical Instrumentation Engineers. One print or electronic copy may be made for personal use only. Systematic reproduction and distribution, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper are prohibited.
The biomechanics of living tissues are critical to normal tissue function and disturbances in these properties are widely implicated in aging and disease. Protein fibres of the extracellular matrix (collagen and elastin) are the fundamental mechanical structures in connective tissues such as bone, cartilage and vasculature. We applied Brillouin light scattering (BLS) spectroscopy and quasistatic stress-strain testing to the study of the mechanics and structure of collagen and elastin fibres purified from connective tissues. BLS probes mechanical properties on a microscopic scale in biological tissues and thereby providing insights into structure–function relationships under normal and pathological conditions. The sensitivity of BLS measurements to fibre structure and hydration was investigated using samples mounted onto reflective substrates. We obtained a complete characterization of the mechanical tensor and elastic moduli which could be compared with complementary data from quasistatic stress-strain measurements at different hydration levels, hence giving the full description of fibre viscoelasticity.
This work was supported by the Engineering and Physical Sciences Research Council [grant number EP/M028739/1].
This is the author accepted manuscript. The final version is available from Society of Photo-optical Instrumentation Engineers (SPIE) via the DOI in this record.
Biophysics, Biology and Biophotonics III: the Crossroads, 27 January - 1 February 2018, San Francisco, US, article 10504