Synthesis of manganese phosphate hybrid nanoflowers by collagen-templated biomineralization

Construction of protein-inorganic hybrid materials with hierarchical nanostructures is critical for the creation of advanced multi-functional materials. We herein for the first time report the synthesis of protein-manganese phosphate hybrid nanomaterials by environmentally amiable biomineralization approach. We have demonstrated that collagen provides an excellent biotemplate to modulate the morphology of the hybrid materials, leading to exquisite nanoflowers with branched petals. In this time-dependent biomineralization process, collagen played an essential role in the production of protein-manganese phosphate hybrid materials by inducing the nucleation of manganese phosphates to form a scaffold as well as serving as a glue to hold the petals together. The as-prepared CL-Mn-3(PO4)(2) nanoflowers exhibited good catalytic activity towards water oxidation. The unique (Gly-X-Y)(n) amino acid sequences and triple helix structure may provide extraordinary capability for collagen to create hybrid nanomaterials via collagen-templated biomineralization. The single-size and high purity may endow recombinant collagen as a powerful strategy to establish superior biotemplates. This facile and green approach to produce collagen-manganese phosphate hybrid nanoflowers greatly advances our capability to construct manganese phosphates-based functional materials.