Considerations regarding the structure of the mammalian mineralized osteoid from viewpoint of the generalized packing model.

The relative magnitudes of mineral, organic and water contents of dense mammalian bone are calculated by a new theory based on recent findings: (1) The neutron diffraction studies of mineralized tissues with different densities demonstrated an inverse relationship between wet density and the equatorial diffraction spacing of the collagen. (2) The neutron studies showed there was very little mineral within the collagen fibrils. (3) A generalized packing model for collagen has been advanced to show how the equatorial spacing can be varied depending on tissue type, water content, and mineral content. (4) The water content of collagen fibrils when calculated from the generalized packing model matches the experimentally determined values for rat tail tendon fibers, bone matrix, and fully mineralized bone. A computational model was developed based on the generalized packing model. It provides a unifying approach to explain many features of mineralized fibrous collagenous tissues. The results are presented as estimates of the mineralized collagen fibril density, the volume fraction of collagen in bone, the density of the extrafibrillar space, the fraction of the e.f. space occupied by mineral and the ratio of mineral within collagen to total mineral content, each expressed as a function of wet bone density. A useful data base, available from previous studies, related mineral, organic and water weight fractions to wet bone density, for a density range from 1.7 g/cc for deer antler to 2.7 g/cc for porpoise petrosal. A second order polynomial was found for each weight fraction component, with bone density as the input variable, with a standard deviation less than 2% of total bone weight. This permits the bone properties to be related to a single variable, the wet bone density. It is seen that compacting the collagen fibrils as well as reducing the organic component weight fraction are two important factors determining the structure of the mineralized osteoid. It was concluded that voids and pore spaces may occupy at least 5% of the bone volume.

[1]  E D Pellegrino,et al.  The chemical anatomy of bone. I. A comparative study of bone composition in sixteen vertebrates. , 1969, The Journal of bone and joint surgery. American volume.

[2]  S. Lees Water content in type i collagen tissues calculated from the generalized packing model , 1986 .

[3]  M. Glimcher Recent studies of the mineral phase in bone and its possible linkage to the organic matrix by protein-bound phosphate bonds. , 1984, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

[4]  S. Lees,et al.  A generalized packing model for type I collagen , 1984 .

[5]  M. Pineri,et al.  Water–collagen interactions: Calorimetric and mechanical experiments , 1978, Biopolymers.

[6]  D. Hulmes,et al.  Molecular packing in collagen , 1981, Nature.

[7]  S. Lees A mixed packing model for bone collagen , 2006, Calcified Tissue International.

[8]  E. P. Katz,et al.  Structure and function of bone collagen fibrils. , 1973, Journal of molecular biology.

[9]  S Lees,et al.  Parameters influencing the sonic velocity in compact calcified tissues of various species. , 1983, The Journal of the Acoustical Society of America.

[10]  H. Mook,et al.  A study of dense mineralized tissue by neutron diffraction , 1984 .

[11]  H. Mook,et al.  Neutron diffraction studies of collagen in fully mineralized bone. , 1985, Journal of molecular biology.

[12]  G. M. Herring CHAPTER 5 – The Organic Matrix of Bone , 1972 .

[13]  P. Timmins,et al.  Collagen–mineral axial relationship in calcified turkey leg tendon by X-ray and neutron diffraction , 1977, Nature.

[14]  D. Hulmes,et al.  Quasi-hexagonal molecular packing in collagen fibrils , 1979, Nature.

[15]  S. Lees,et al.  Density of a sample bovine cortical bone matrix and its solid constituent in various media , 2006, Calcified Tissue International.

[16]  J. Vaughan THE PHYSIOLOGY OF BONE , 1970, The Ulster Medical Journal.

[17]  P. Gallop,et al.  Cross-linking in collagen and elastin. , 1984, Annual review of biochemistry.