AFM study of morphology and mechanical properties of a chimeric spider silk and bone sialoprotein protein for bone regeneration

Biomacromolecules. 2011 May 9;12(5):1675-85. doi: 10.1021/bm2000605. Epub 2011 Mar 31.

Abstract

Atomic force microscopy (AFM) was used to assess a new chimeric protein consisting of a fusion protein of the consensus repeat for Nephila clavipes spider dragline protein and bone sialoprotein (6mer+BSP). The elastic modulus of this protein in film form was assessed through force curves, and film surface roughness was also determined. The results showed a significant difference among the elastic modulus of the chimeric silk protein, 6mer+BSP, and control films consisting of only the silk component (6mer). The behavior of the 6mer+BSP and 6mer proteins in aqueous solution in the presence of calcium (Ca) ions was also assessed to determine interactions between the inorganic and organic components related to bone interactions, anchoring, and biomaterial network formation. The results demonstrated the formation of protein networks in the presence of Ca(2+) ions, characteristics that may be important in the context of controlling materials assembly and properties related to bone formation with this new chimeric silk-BSP protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biocompatible Materials
  • Bone Regeneration*
  • Bone and Bones / chemistry*
  • Circular Dichroism
  • Cloning, Molecular
  • Microscopy, Atomic Force
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Recombinant Fusion Proteins / chemistry*
  • Recombinant Fusion Proteins / genetics
  • Sialoglycoproteins / chemistry*
  • Sialoglycoproteins / genetics
  • Silk / chemistry*
  • Spiders

Substances

  • Biocompatible Materials
  • Recombinant Fusion Proteins
  • Sialoglycoproteins
  • Silk