Abstract
Taking lessons from the structure-forming process of biominerals in animals and plants, one can find tremendous inspirations and ideas for developing advanced synthesis techniques, which is called bio-process inspired synthesis. Bone, as a typical representative of biominerals, is constituted of mineralized collagen fibrils, which are formed under the functions of non-collagenous proteins (NCPs). Intrafibrillar mineralization is the consequence of a synergy among several NCPs. In the present study, we have designed a multi-functional protein, named (MBP)-BSP-HAP, based on bone sialoprotein (BSP) and hydroxyapatite binding protein (HAP), to mimic the intrafibrillar mineralization process in vitro. The three functional domains of (MBP)-BSP-HAP provide the artificial protein with multiple designated functions for intrafibrillar mineralization including binding calcium ions, binding collagen, and binding hydroxyapatite. Platelet-like hydroxyapatite crystals periodically arranged inside the collagen fibrils have been achieved under the function of (MBP)-BSP-HAP. The mechanism of intrafibrillar mineralization directed by the multi-functional protein was proposed. This work may not only shed light on bio-process inspired approaches for more economic and efficient biomimetic synthesis, but also be helpful in understanding the natural process of bone formation for bone regeneration and tissue repair.
Original language | English |
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Pages (from-to) | 4496-4502 |
Number of pages | 7 |
Journal | Journal of Materials Chemistry C |
Volume | 3 |
Issue number | 22 |
DOIs | |
Publication status | Published - 14 Jun 2015 |
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Physical Chemistry and characterization(PC2)
Johan Wouters (Manager) & Carmela Aprile (Manager)
Technological Platform Physical Chemistry and characterizationFacility/equipment: Technological Platform