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Bioengineering of the silica-polymerizing enzyme silicatein-alpha for a targeted application to hydroxyapatite.

Abstract：

:Since its discovery, numerous biotechnological approaches have aimed to explore the silica-polymerizing catalytic activity of the enzyme silicatein. In vivo, silicatein catalyzes polymerization of amorphous silica nanospheres from soluble precursors. In vitro, it directs the formation of nanostructured biosilica. This is of interest for various applications that strive to benefit from both the advantages of the biological system (i.e., silica synthesis under physiological conditions) and the cell mineralization-stimulating effect of biosilica. However, so far immobilization of silicatein has been hampered by the complex multistep procedure required. In addition, the chemical surface modifications involved not only restrict the choice of carrier materials but also render application of silicatein to hydroxyapatite (HA) of mineralized tissue impossible. Here we describe the bioengineering of silicatein, adapted for application in the fields of bone regeneration, tissue engineering, and dental care. Inspired by Glu-rich sequences of mammalian proteins that confer binding affinity to HA, a novel protein-tag was developed, the Glu-tag. Following expression of Glu-tagged silicatein, the HA-binding capacity of the enzyme is demonstrated in combination with synthetic and dental HA. Furthermore, immobilized Glu-tagged silicatein catalyzes synthesis of biosilica coatings on both synthetic HA nanofibrils and dental HA. Hence, Glu-tagged silicatein reveals a considerable biomedical potential with regenerative and prophylactic implementations.

journal_name

Acta Biomater

journal_title

Acta biomaterialia

authors

Natalio F,Link T,Müller WE,Schröder HC,Cui FZ,Wang X,Wiens M

doi

10.1016/j.actbio.2010.03.010

subject

Has Abstract

pub_date

2010-09-01 00:00:00

pages

3720-8

issue

9

eissn

1742-7061

issn

1878-7568

pii

S1742-7061(10)00136-4

journal_volume

6

pub_type

杂志文章

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