Research article summary (published 10 Jun 2006):

Novel nanocomposites from spider silk-silica fusion (chimeric) proteins.

Full 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.

Author information

Author/s: Wong Po Foo, Cheryl (C); Patwardhan, Siddharth V (SV); Belton, David J (DJ); Kitchel, Brandon (B); Anastasiades, Daphne (D); Huang, Jia (J); Naik, Rajesh R (RR); Perry, Carole C (CC); Kaplan, David L (DL);

Affiliation: Department of Biomedical Engineering, Bioengineering and Biotechnology Center, Tufts University, Medford, MA 02155, USA.

Grants: EB 000252 (Agency:NIBIB NIH HHS) ; EB 003210 (Agency:NIBIB NIH HHS)

Journal and publication information

Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.

Journal: Proceedings of the National Academy of Sciences of the United States of America (Proc Natl Acad Sci U S A), published in United States. (Language: eng)

Reference: 2006-Jun; vol 103 (issue 25) : pp 9428-33

Dates: Created 2006/06/21; Completed 2006/08/14; Revised 2008/11/20;

PMID: 16769898, status: MEDLINE (last retrieval date: 2/18/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

External Links for this article
(including full text providers, if available):

Click Electronic Full-text Provider Links to see options for finding the electronic full text links to this article. Note there may be a subscription or fee required for access to the full text. See our FAQ for information on finding FREE full text articles.

This article may also be located in paper journal collections available in many libraries. Use the Journal and Publication Information above to find the full article.

MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Amino Acid Sequence Animals Fibroins - chemistry; genetics; isolation & purification; metabolism Insect Proteins - chemistry; genetics; isolation & purification; metabolism Microscopy, Electron, Scanning Molecular Sequence Data

Nanostructures - chemistry; ultrastructure Recombinant Fusion Proteins - genetics; isolation & purification; metabolism Sequence Alignment Silicon Dioxide - chemistry Silk - chemistry; genetics; isolation & purification; metabolism Spiders - chemistry

Associated Chemicals: Insect Proteins (0) ; Recombinant Fusion Proteins (0) ; Silk (0) ; spidroin 1 (0) ; Silicon Dioxide (7631-86-9) ; Fibroins (9007-76-5)

Related articles

These are the highest related articles currently in the database:

• [A study of periodicity in the primary structure of spidroin 1 and spidroin 2 from spiders belonging to various species] 30 Oct 2004
• Molecular mechanisms of spider silk. 30 Aug 2006
• Inter-specific sequence conservation and intra-individual sequence variation in a spider silk gene. 29 Sep 2004
• Molecular characterization and evolutionary study of spider tubuliform (eggcase) silk protein. 5 Jun 2005
• Identification and characterization of multiple Spidroin 1 genes encoding major ampullate silk proteins in Nephila clavipes. 30 Aug 2008
• Composition and hierarchical organisation of a spider silk. Oct 2007
• Characterization and expression of a cDNA encoding a tubuliform silk protein of the golden web spider Nephila antipodiana. 27 Mar 2006
• The effect of genetically engineered spider silk-dentin matrix protein 1 chimeric protein on hydroxyapatite nucleation. 5 Feb 2007
• Environmental conditions impinge on dragline silk protein composition. 30 Aug 2008
• [An analysis of the secondary structure of spider spidroins I and II belonging to different species] 30 Oct 2004

See 100+ related articles.

Related Article Map

Legend: - FREE Full text Article. - Abstract only. - Title only. More help.

See a large map of 100+ related articles.