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• W2897776209 endingPage "20180269" @default.
• W2897776209 startingPage "20180269" @default.
• W2897776209 abstract "Formation of hydroxyapatite (HAP) within collagen fibrils, as found in bone, dentine and cementum, is thought to be mediated by proteins rich in aspartate (Asp) and glutamate such as osteopontin and bone sialoprotein, respectively. Indeed polyaspartate (pAsp), a homopolymer analogue of such proteins, has been shown to induce intrafibrillar mineralization of collagen from solutions of calcium and phosphate that are supersaturated with respect to HAP. To elucidate the role of pAsp in mineralization of collagen, we explored the effect of pAsp chain length on in vitro HAP deposition in demineralized mouse periodontal tissue sections. Through characterization of both tissue sections and mineralizing solution, we show that chain length contributes to the effectiveness of pAsp in mediating intrafibrillar mineralization. This function appears to be associated with inhibition of otherwise kinetically favoured crystallization in the bulk solution, which allows for intrafibrillar crystallization, though this does not preclude the possibility of a more active role for pAsp in addition. Inhibition of crystallization in solution by pAsp occurs by slowing the growth of amorphous calcium phosphate and stabilization of this phase, rather than by sequestration of Ca 2+ ions. These results suggest that the length of Asp-rich sequences of mineralizing proteins may be essential to their function, and could also be useful in optimization of mineralized tissue replacement synthesis." @default.
• W2897776209 created "2018-10-26" @default.
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• W2897776209 date "2018-10-01" @default.
• W2897776209 modified "2023-10-02" @default.
• W2897776209 title "The effect of polyaspartate chain length on mediating biomimetic remineralization of collagenous tissues" @default.
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• W2897776209 doi "https://doi.org/10.1098/rsif.2018.0269" @default.
• W2897776209 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6228489" @default.
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