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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Wong Po Foo, Cheryl Patwardhan, Siddharth V. Anastasiades, Daphne Naik, Rajesh R. Belton, David J. Kaplan, David L. Kitchel, Brandon Huang, Jia Perry, Carole C. |
| Description | Author Affiliation: Wong Po Foo C ( Department of Biomedical Engineering, Bioengineering and Biotechnology Center, Tufts University, Medford, MA 02155, USA.); |
| Abstract | Silica skeletal architectures in diatoms are characterized by remarkable morphological and nanostructural details. Silk proteins from spiders and silkworms form strong and intricate self-assembling fibrous biomaterials in nature. We combined the features of silk with biosilica through the design, synthesis, and characterization of a novel family of chimeric proteins for subsequent use in model materials forming reactions. The domains from the major ampullate spidroin 1 (MaSp1) protein of Nephila clavipes spider dragline silk provide control over structural and morphological details because it can be self-assembled through diverse processing methods including film casting and fiber electrospinning. Biosilica nanostructures in diatoms are formed in aqueous ambient conditions at neutral pH and low temperatures. The R5 peptide derived from the silaffin protein of Cylindrotheca fusiformis induces and regulates silica precipitation in the chimeric protein designs under similar ambient conditions. Whereas mineralization reactions performed in the presence of R5 peptide alone form silica particles with a size distribution of 0.5-10 microm in diameter, reactions performed in the presence of the new fusion proteins generate nanocomposite materials containing silica particles with a narrower size distribution of 0.5-2 microm in diameter. Furthermore, we demonstrate that composite morphology and structure could be regulated by controlling processing conditions to produce films and fibers. These results suggest that the chimeric protein provides new options for processing and control over silica particle sizes, important benefits for biomedical and specialty materials, particularly in light of the all aqueous processing and the nanocomposite features of these new materials. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 25 |
| Volume Number | 103 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2006-06-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Fibroins Chemistry Metabolism Insect Proteins Nanostructures Silicon Dioxide Silk Spiders Amino Acid Sequence Animals Genetics Isolation & Purification Microscopy, Electron, Scanning Molecular Sequence Data Ultrastructure Recombinant Fusion Proteins Sequence Alignment Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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