Studying the Function of Pyriform Spidroin-2 Modules
Poster Number
64
Format
Poster Presentation
Faculty Mentor Name
Craig Vierra
Faculty Mentor Department
Biological Sciences
Abstract/Artist Statement
Extensive research on the properties of spider silk has sparked the interests of the general community in discovering potential uses for these materials. Mechanical properties have shown that the strength of spider silk is comparable to that of high-tensile steel. When comparing other properties, spider silk is more extensible and tougher relative to high-tensile steel and Kevlar. With such superb mechanical properties, spider silk is being further studied for future industrial uses. Pyriform Spidroin 2 (PySp2) is a glue silk fibroin spun by orb-weaving spiders from the pyriform gland. PySp2 is spun into attachment discs as a viscous liquid that dries rapidly, allowing for the fastening of dragline silk, which facilitates locomotion and web construction. The internal block-repeat sequences of PySp2 have the ability to self-assemble, promoting fiber formation to occur in a liquid environment. The PySp2 protein sequences play a central role in affecting the protein’s overall mechanical properties. The goal of our research was to express truncated versions of PySp2 proteins in bacteria and spin fibers from these purified proteins in order to test its mechanical properties. To express the proteins, the PySp2 cDNA was inserted into the cloning vector pBAD-Thio- TOPO, which was propagated in bacteria. Bacterial cells carrying the expression vector were induced and the resulting recombinant proteins were further studied. Western blot analysis was used to verify the expression of the protein. Results showed that PySp2 recombinant proteins were expressed in bacteria, specifically in cells carrying the expression vectors with the PySp2 cDNA. These positive results will allow further experimentation and observation of the mechanical properties of glue silk fibers spun from the purified proteins.
Location
Grave Covell
Start Date
21-4-2012 10:00 AM
End Date
21-4-2012 12:00 PM
Studying the Function of Pyriform Spidroin-2 Modules
Grave Covell
Extensive research on the properties of spider silk has sparked the interests of the general community in discovering potential uses for these materials. Mechanical properties have shown that the strength of spider silk is comparable to that of high-tensile steel. When comparing other properties, spider silk is more extensible and tougher relative to high-tensile steel and Kevlar. With such superb mechanical properties, spider silk is being further studied for future industrial uses. Pyriform Spidroin 2 (PySp2) is a glue silk fibroin spun by orb-weaving spiders from the pyriform gland. PySp2 is spun into attachment discs as a viscous liquid that dries rapidly, allowing for the fastening of dragline silk, which facilitates locomotion and web construction. The internal block-repeat sequences of PySp2 have the ability to self-assemble, promoting fiber formation to occur in a liquid environment. The PySp2 protein sequences play a central role in affecting the protein’s overall mechanical properties. The goal of our research was to express truncated versions of PySp2 proteins in bacteria and spin fibers from these purified proteins in order to test its mechanical properties. To express the proteins, the PySp2 cDNA was inserted into the cloning vector pBAD-Thio- TOPO, which was propagated in bacteria. Bacterial cells carrying the expression vector were induced and the resulting recombinant proteins were further studied. Western blot analysis was used to verify the expression of the protein. Results showed that PySp2 recombinant proteins were expressed in bacteria, specifically in cells carrying the expression vectors with the PySp2 cDNA. These positive results will allow further experimentation and observation of the mechanical properties of glue silk fibers spun from the purified proteins.