2018
DOI: 10.1016/j.bone.2018.02.022
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Bone toughness at the molecular scale: A model for fracture toughness using crosslinked osteopontin on synthetic and biogenic mineral substrates

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Cited by 26 publications
(21 citation statements)
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“…Interestingly, many of the non-collagenous proteins that produce fracture resistance (toughness) in bone are highly phosphorylated peptides that are also involved in load dissipation, as well as interfacial adhesion, between the organic and inorganic phases of bone [42]. Osteopontin is a non-collagenous component of the osteoid with large amounts of (>10% of total amino acids) phosphorylated serine residues [43] that increases the fracture toughness of bones [44,45,46]. Osteopontin also produces an adhesive effect at the atomic to nanoscale [29,47,48] by crosslinking via ionic bonding with calcium [42,47,49].…”
Section: Introductionmentioning
confidence: 99%
“…Interestingly, many of the non-collagenous proteins that produce fracture resistance (toughness) in bone are highly phosphorylated peptides that are also involved in load dissipation, as well as interfacial adhesion, between the organic and inorganic phases of bone [42]. Osteopontin is a non-collagenous component of the osteoid with large amounts of (>10% of total amino acids) phosphorylated serine residues [43] that increases the fracture toughness of bones [44,45,46]. Osteopontin also produces an adhesive effect at the atomic to nanoscale [29,47,48] by crosslinking via ionic bonding with calcium [42,47,49].…”
Section: Introductionmentioning
confidence: 99%
“…Such a feature, which accounts for the increased resilience and high work of fracture of biomineralized collagen-based tissues ( 35 ), may be attributed to the cross-linking of HPAA, which acts as cohesive/adhesive “binders” for the collagen/mineral composite hybrid. Similar to cross-linked osteopontin found in the bone ( 36 ), the bound HPAA may provide a binding layer between the intrafibrillarly mineralized collagen and the extrafibrillar minerals, which enhances interfacial adhesion and the fracture toughness of the material.…”
Section: Resultsmentioning
confidence: 90%
“…They discovered the presence of a non-fibrillar organic matrix based on non-collagenous proteins (NCP) mainly composed of osteopontin (OPN), which acts as a glue that holds the mineralized fibrils together. Recently, Cavalier et al [70] discovered an important mechanism suggesting that OPN crosslinking enhances the interfacial organic-inorganic adhesion, hence increases the fracture toughness of bone. The effectiveness of this mechanism increases with the presence of Ca 2+ ions.…”
Section: Structure-functionmentioning
confidence: 99%