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.
journal_name
Biomacromoleculesjournal_title
Biomacromoleculesauthors
Gomes S,Numata K,Leonor IB,Mano JF,Reis RL,Kaplan DLdoi
10.1021/bm2000605subject
Has Abstractpub_date
2011-05-09 00:00:00pages
1675-85issue
5eissn
1525-7797issn
1526-4602journal_volume
12pub_type
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