Neutron diffraction studies of collagen in fully mineralized bone

Bonar, Laurence C.; Lees, Sidney; Mook, H. A.

doi:10.1016/0022-2836(85)90090-7

Cited by 180 publications

(131 citation statements)

References 23 publications

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“…We calculate that ~68.8% of the mineral is extrafibrillar in the ordered phase and 77.9% in the disordered phase. This falls in line with the literature that suggests most the mineral is located outside the fibril 9,13 . Although this model only considered dry bone, it is noteworthy that the is just the percentage of total mineral fraction that is outside the fibril and thus could remain constant even if decreased once water is introduced.…”

Section: Mf Modelsupporting

confidence: 92%

The nanocomposite nature of bone drives its strength and damage resistance

2016

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Crystallization of ACP with timeTo probe the stability of the observed ACP in disordered phase with respect to the adjacent HA nanocrystals, we performed TEM analysis of the same region after a 30-day time lapse. During the 30 days, the TEM sample was stored at room temperature in a N2 environment. Figure S1a shows the initial arrangement of ACP (left) and HA nanocrystals (right), as well as the diffraction pattern inset showing the crystallinity of the HA. Figure S1b shows the same region after the 30 day incubation period; the HA nanocrystals on the right appear to have grown, confirmed by the increased (112), (211), (300) intensities in the diffraction pattern inset; we also observe the emergence of (002) reflections after one month, which further proves the formation of crystals. These results demonstrate suggest that biogenic ACP is a precursor for crystalline cHA formation in bone in the observed conditions, as similarly observed by Mahamid et al 1 . Figure S1. Time lapse micrographs of amorphous and nanocrystalline regions. Deprotonated mineral structure in disordered phase taken before (a) and after (b) a 30 day incubation at room temperature in a nitrogen environment. The electron diffraction pattern after the incubation (b, inset) shows an increase in crystallinity as evidenced by more intense HA reflections and the emergence of the (002) spots when compared to the initial diffraction pattern (a, inset). Size Dependent Model ConstructionWe propose that the yield strength, , decreases as the probability of having a flaw (i.e. a pore) on the pillar surface increases; that is, surface flaws serve as probabilistic stress concentrators, which initiate failure during compression. This is manifested most prevalently in the larger pillars, with diameters > 500nm. At these nano and micro length scales, it is reasonable to consider bone as a fiber-

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Section: Mf Modelsupporting

confidence: 92%

The nanocomposite nature of bone drives its strength and damage resistance

2016

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“…Neutron scattering experiments in adult bovine samples corroborate this premise with the radial distance between collagen molecules in wet mineralized bone measured to be 1.24 nm which is substantially lower compared to the 1.53 nm measured in wet demineralized bone [38]. This suggests that, in the absence of external macroscopic volume changes, the collagen matrix has to compress to accommodate the growth of the mineral crystals.…”

Section: Discussionsupporting

confidence: 66%

Characterising Bone Material Composition and Structure in the Ovariectomized (OVX) Rat Model of Osteoporosis

et al. 2015

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“…The collagen location of this water is supported by the fact that an 80-ml volume of water is calculated to lie within the collagen of the demineralized bone column (see "Results" and Table 4). The fibril location of this collagen water is in turn supported by x-ray diffraction studies that show that hydration produces a comparable increase in the Bragg spacing of collagen molecules in the lateral plane of tendon and demineralized bone collagen fibrils (40).…”

Section: Test Molecule Massmentioning

confidence: 76%

The Size Exclusion Characteristics of Type I Collagen

Toroian

Lim

Price

2007

Journal of Biological Chemistry

219

113

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The mineral in bone is located primarily within the collagen fibril, and during mineralization the fibril is formed first and then water within the fibril is replaced with mineral. The collagen fibril therefore provides the aqueous compartment in which mineral grows. Although knowledge of the size of molecules that can diffuse into the fibril to affect crystal growth is critical to understanding the mechanism of bone mineralization, there have been as yet no studies on the size exclusion properties of the collagen fibril. To determine the size exclusion characteristics of collagen, we developed a gel filtration-like procedure that uses columns containing collagen from tendon and bone. The elution volumes of test molecules show the volume within the packed column that is accessible to the test molecules, and therefore reveal the size exclusion characteristics of the collagen within the column. These experiments show that molecules smaller than a 6-kDa protein diffuse into all of the water within the collagen fibril, whereas molecules larger than a 40-kDa protein are excluded from this water. These studies provide an insight into the mechanism of bone mineralization. Molecules and apatite crystals smaller than a 6-kDa protein can diffuse into all water within the fibril and so can directly impact mineralization. Although molecules larger than a 40-kDa protein are excluded from the fibril, they can initiate mineralization by forming small apatite crystal nuclei that diffuse into the fibril, or can favor fibril mineralization by inhibiting apatite growth everywhere but within the fibril.

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Neutron diffraction studies of collagen in fully mineralized bone

Cited by 180 publications

References 23 publications

The nanocomposite nature of bone drives its strength and damage resistance

The nanocomposite nature of bone drives its strength and damage resistance

Characterising Bone Material Composition and Structure in the Ovariectomized (OVX) Rat Model of Osteoporosis

The Size Exclusion Characteristics of Type I Collagen

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