Hierarchical and non-hierarchical mineralisation of collagen.
Biomineralisation of collagen involves functional motifs incorporated in extracellular matrix protein molecules to accomplish the objectives of stabilising amorphous calcium phosphate into nanoprecursors and directing the nucleation and growth of apatite within collagen fibrils. Here we report the use of small inorganic polyphosphate molecules to template hierarchical intrafibrillar apatite assembly in reconstituted collagen in the presence of polyacrylic acid to sequester calcium and phosphate into transient amorphous nanophases. The use of polyphosphate without a sequestration analogue resulted only in randomly-oriented extrafibrillar precipitations along the fibrillar surface. Conversely, the use of polyacrylic acid without a templating analogue resulted only in non-hierarchical intrafibrillar mineralisation with continuous apatite strands instead of discrete crystallites. The ability of using simple non-protein molecules to recapitulate different levels of structural hierarchy in mineralised collagen signifies the ultimate simplicity in Nature's biomineralisation design principles and challenges the need for using more complex recombinant matrix proteins in bioengineering applications.
Department of Stomatology, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
Yan
Y
Liu
Young-Kyung
YK
Kim
Lin
L
Dai
Nan
N
Li
Sara O
SO
Khan
David H
DH
Pashley
Franklin R
FR
Tay
D001672:Biocompatible Materials / Q000737:chemistry*; D002130:Calcium Phosphates / Q000737:chemistry; D003094:Collagen / Q000737:chemistry*; D046529:Microscopy, Electron, Transmission; D017550:Spectroscopy, Fourier Transform Infrared
D001672:Biocompatible Materials; D002130:Calcium Phosphates; C519480:amorphous calcium phosphate; D003094:Collagen