bei Google ScholarTitelangaben
Neubauer, Vanessa ; Scheibel, Thomas:
Spider Silk Fusion Proteins for Controlled Collagen Binding and Biomineralization.
In: ACS Biomaterials Science & Engineering.
Bd. 6
(2020)
Heft 10
.
- S. 5599-5608.
ISSN 2373-9878
DOI: https://doi.org/10.1021/acsbiomaterials.0c00818
Abstract
The development of biomaterials for the interfacebetween tendon and bone is important for realizing functional tendonreplacements. Toward the development of new materials for suchapplications, engineered recombinant spider silk proteins were modifiedwith peptide tag sequences derived from noncollagenous proteins inbone, so-called SIBLING proteins, such as osteopontin and sialoprotein,which are known to interact with collagen and to initiate mineralization.Materials made of these spider silk−SIBLING hybrids were analyzedconcerning mineralization and interaction with cells. They showedenhanced calcium phosphate formation upon incubation in mineraliza-tion agents. In gradientfilms, MC3T3-E1 mouse preosteoblasts adheredpreferentially along the gradient toward the variant with a collagen binding motif.