A novel route for immobilization of proteins to silica particles incorporating silaffin domains

Title
A novel route for immobilization of proteins to silica particles incorporating silaffin domains
Authors
남동현원기훈김용환상병인
Keywords
Bionano; Silicifiction; silaffin polypeptide; protein immobilization; R1 peptide
Issue Date
2009-12
Publisher
Biotechnology progress
Citation
VOL 25, NO 6, 1643-1649
Abstract
In the diatom Cylindrotheca fusiformis, modified peptides called silaffin polypeptides are responsible for silica deposition in vivo at ambient conditions. Recently, it was discovered that the synthetic R5 peptide, the repeat unit of silaffin polypeptide without post-translational modification, was capable of precipitating silica in vitro and at ambient conditions. Herein, chimeric proteins were generated by incorporating synthetic silaffin R5 peptides and related unmodified silaffin domains (R1-R7) from Cylindrotheca fusiformis onto green fluorescent protein (GFP) by recombinant DNA technology and their ability to cause silicification was also examined. GFP chimeric proteins showed silicification at very low concentrations (600-700 g/mL) when compared with adding excess amounts of R5 peptides (10 mg/mL) as previously reported. Sensitive to pH conditions, only the GFP-R1 chimera showed silicification activity at pH 8.0. The protein immobilization efficiencies of these chimeras were unexpectedly high ranging from 75 to 85%, with the R1 silaffin-protein construct showing excellent immobilization efficiency and a constant molar ratio of silica to protein ranging from 250 to 350 over a wide pH range. The average silica particle sizes had a tendency to decrease as pH increased to basic conditions. This study demonstrated the production of nanoscale immobilized protein, fabricated via silaffin-fused proteins.
URI
http://pubs.kist.re.kr/handle/201004/36376
ISSN
8756-7938
Appears in Collections:
KIST Publication > Article
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