Frandsen, Paul; Bursell, Madeline; Taylor, Adam; Wilson, Seth; Steeneck, Amy; Stewart, Russell (Brigham Young University)
Faculty Advisor: Frandsen, Paul (Life Sciences, Plant and Wildlife Sciences)
Caddisfly (Insecta: Trichoptera) silk is unique from other insect's silk in that it retains its adhesive capabilities, strength and viscoelasticity when submerged in water. To understand how caddisfly silk is capable of possessing these characteristics, it is essential to understand the protein foundation of the silk proteins. Caddisfly silk is complex and made up of different structures generated by processes that are unique to caddisfly silk. H-Fibroin and L-Fibroin have been identified as two of the major protein components within caddisfly silk (Hatano & Nagashima, 2015). The caddisfly silk fibre experiences unique structures not typically seen in nature. An understanding of the primary structure of the silk fibre is essential in understanding the complexity of the silk's capabilities. In this study, we used proteomic techniques to analyze the complex H-Fibroin protein and the silk fibre in order to look at the underlying structural features of the protein. In doing so, we identified post-translational phosphorylation, metal cation incorporation, and other structural features which contributes to Caddisfly silk's adhesive capabilities, strength and viscoelasticity when submerged in water.