title: Do stress-whitening and optical clearing of collagenous tissue occur by the same mechanism?
abstract: Bone is biphasic with an organic matrix and an inorganic mineral component. As we age bone's susceptibility to fracture increases. It has been shown that there is no change in mean mineralization with aging, but bone nevertheless becomes less tough. This aging effect is therefore likely related to the organic phase. Under mechanical loading, immediately prior to failure, bone has been observed to visually become more opaque and has been termed stress-whitening. Stress-whitening is known to make materials tougher. The goal of this investigation was to investigate stress-whitening in the collagenous matrix of bone. Hydrogen bonds play a key role in collagen stability and we hypothesize that changes in hydrogen bonding will significantly affect matrix stiffness, toughness and stress whitening. Demineralized bone specimens were loaded in tension and stress-whitening was monitored. The effect of hydrogen bonding on mechanical properties and stress-whitening process was probed by altering the Hansen's hydrogen bonding parameter (δh) of the immersing solution. The Hansen's hydrogen bonding parameter of the immersing fluid affected the morphology, mechanical properties and stress whitening of specimens. Specimens were visually whiter in the absence of mechanical load in low δh solvents (the specimens solvent-whitened). Both the observed stress-whitening and solvent-whitening were reversible and repeatable processes. The observed solvent-whitening that occurred without the presence of load was consistent with solvent-induced optical clearing (the opposite of whitening) in skin caused by collagen fibril swelling. Stress whitening and solvent whitening can be explained by a common mechanism, collagen fibril densification and thinning, leading to an increased distinction between the collagen fibrillar phase and immersing fluid, ultimately leading to more scattering. Bones may be at a greater risk for fracture as we age because solubility of the matrix changes, thus making the collagen less hydrated (and more brittle) even in the same solvent.
authors: Lawrence J. Ellison Musculoskeletal Research Laboratory, Department of Orthopaedic Surgery, UC Davis School of Medicine & Biomedical Engineering Graduate Group, UC Davis, United States. Electronic address: mrhardisty@ucdavis.edu.
authors: M R
authors: MR
authors: Hardisty
authors: M A
authors: MA
authors: Soicher
authors: T C
authors: TC
authors: Garcia
authors: S M
authors: SM
authors: Stover
authors: D P
authors: DP
authors: Fyhrie
mesh_terms: D000818:Animals; D003094:Collagen / Q000737:chemistry / Q000502:physiology*; D055119:Elastic Modulus; D000431:Ethanol / Q000737:chemistry; D005561:Formates / Q000737:chemistry; D006736:Horses; D006860:Hydrogen Bonding; D050279:Metacarpal Bones / Q000737:chemistry / Q000503:physiopathology*; D012997:Solvents / Q000737:chemistry; D013314:Stress, Mechanical
chemical_list: D005561:Formates; D012997:Solvents; C030544:formic acid; D000431:Ethanol; D003094:Collagen
keywords: Biomechanics; Cortical bone; Hansen's hydrogen bonding potential; Optical clearing; Optics; Stress-induced whitening