Falconer and Christopher Gallego-Lazo, undergraduate researchers in the lab of Andrew Smith, PhD, at Ithaca College, will present their research at the American Society for Biochemistry and Molecular Biology annual meeting.
Falconer analyzed 11 proteins unique to the slug glue that were previously identified by Smith's research team. Using recombinant DNA technology, she produced abundant amounts of each protein for analysis. The techniques she developed could also be used to reproduce the proteins for a manmade glue.
The analysis revealed that some of the proteins tend to bind to themselves or with other proteins to form a three-dimensional network. These findings suggest that this oligomerization may be required for some of the proteins to be most functional.
Gallego-Lazo's study focused on understanding the double network structure that makes the slug glue highly deformable but able to withstand large amounts of force. The glue has a stiff protein network that uses sacrificial bonds to absorb energy, protecting an intertwined deformable network of carbohydrates.
Gallego-Lazo discovered that changing specific chemical bonds within the slug glue's protein network modified the glue's strength. These bonds can be reformed naturally, enabling the glue to deform while maintaining its strength.
"Few studies on biological adhesives have identified the exact nature of the bonds holding the glue together," said Gallego-Lazo. "This knowledge can guide the development of an organic synthetic adhesive that would reduce the risk of infection and scarring compared to stitches and staples and could be applied rapidly and simply."
COMPAMED-tradefair.com; Source: Experimental Biology
