Biomedical Engineering Reference
In-Depth Information
integrin binding specificity can be conveyed by engineering ligands that
recapitulate the secondary and tertiary structure of the natural biopoly-
mers (Fig. 6). The improved activity/selectivity of these “second-generation”
biomolecular interfaces enhances the therapeutic and biotechnological po-
tential of biomimetic materials.
Fig. 6
Ligands with secondary/tertiary structure promote binding of
α
2
β
1
integrin, a non-
RGD binding integrin.
A
Diagram showing strategy for presenting collagen-mimetic,
triple-helical GFOGER peptide.
B
Tethering of GFOGER onto nonfouling surfaces sup-
ports cell adhesion comparable to COL-I, and adhesion is completely blocked by anti-
bodies against
α
2
β
1
integrin.
C
Equivalent levels of matrix mineralization for osteoblasts
grown on GFOGER-functionalized and COL-I-coated surfaces. Adapted from [87, 88]
