abstract: An animal's ability to produce protein-based silk materials has evolved independently in many different arthropod lineages, satisfying various ecological necessities. However, regardless of their wide range of uses and their potential industrial and biomedical applications, advanced knowledge on the molecular structure of silk biopolymers is largely limited to those produced by spiders (order Araneae) and silkworms (order Lepidoptera). This thesis provides an in-depth molecular-level characterization of silk fibers produced by two vastly different insects: the caddisfly larvae (order Trichoptera) and the webspinner (order Embioptera).
The molecular structure of caddisfly larval silk from the species <italic>Hesperophylax consimilis</italic> was characterized using solid-state nuclear magnetic resonance (ss-NMR) and Wide Angle X-ray Diffraction (WAXD) techniques. This insect, which typically dwells in freshwater riverbeds and streams, uses silk fibers as a strong and sticky nanoadhesive material to construct cocoons and cases out available debris. Conformation-sensitive <super>13</super>C chemical shifts and <super>31</super>P chemical shift anisotropy (CSA) information strongly support a unique protein motif in which phosphorylated serine- rich repeats (pSX)<sub>4</sub> complex with di- and trivalent cations to form rigid nanocrystalline β-sheets. Additionally, it is illustrated through <super>31</super>P NMR and WAXD data that these nanocrystalline structures can be reversibly formed, and depend entirely on the presence of the stabilizing cations.
Nanofiber silks produced by webspinners (order Embioptera) were also studied herein. This work addresses discrepancies in the literature regarding fiber diameters and tensile properties, revealing that the nanofibers are about 100 nm in diameter, and are stronger (around 500 MPa mean ultimate stress) than previous works suggested. Fourier-transform Infrared Spectroscopy (FT-IR), NMR and WAXD results find that approximately 70% of the highly repetitive glycine- and serine-rich protein core is composed of β-sheet nanocrystalline structures. In addition, FT-IR and Gas-chromatography mass spectroscopy (GC-MS) data revealed a hydrophobic surface coating rich in long-chain lipids. The effect of this surface coating was studied with contact angle techniques; it is shown that the silk sheets are extremely hydrophobic, yet due to the microstructural and nanostructural details of the silk surface, are surprisingly adhesive to water. / Dissertation/Thesis / Doctoral Dissertation Biochemistry 2014
Identifer | oai:union.ndltd.org:asu.edu/item:25937 |
Date | January 2014 |
Contributors | Addison, John Bennett (Author), Yarger, Jeffery L (Advisor), Holland, Gregory P (Advisor), Wang, Xu (Committee member), Ros, Robert (Committee member), Arizona State University (Publisher) |
Source Sets | Arizona State University |
Language | English |
Detected Language | English |
Type | Doctoral Dissertation |
Format | 188 pages |
Rights | http://rightsstatements.org/vocab/InC/1.0/, All Rights Reserved |
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