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Date of Award
Department or Program Affiliation
Master of Science (MS)
Murphy, Amanda R.
Larsen, Michael B.
Antos, John M.
Thiolated polymers, or thiomers, have demonstrated advanced adhesion to biological surfaces such as mucus membranes due to their ability to form disulfide bonds to the cysteine-rich domains in mucin making them an attractive drug delivery system. Silk fibroin, a protein derived from the Bombyx mori silkworm, offers a biocompatible and biodegradable platform absent in other thiomer systems. However, due to the small percentage of native cysteine residues in silk, installation of additional thiols is essential to create an advanced thiomer adhesive. In this research, covalent attachment of non-native thiols to the tyrosine residues of silk fibroin is accomplished with a high degree of functionalization. The extent of thiol modification is characterized by ultraviolet-visible spectroscopy (UV-VIS), proton nuclear magnetic resonance spectroscopy (1H NMR), and 1H-15N heteronuclear multiple bond correlation (HMBC). The reactivity of the thiol handles are probed using fluorescence spectroscopy and the in situ gelling ability of the thiolated silk is investigated using infrared spectroscopy (IR) and rheological measurements.
Silk, tyrosine, disulfide, thiol, mucoadhesion, crosslinking, gel
Western Washington University
Subject – LCSH
Polymers; Cysteine; Thiols--Synthesis; Silk--Biocompatibility; Silk--Biodegradation
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Talusig, Jeremy Martinez, "Synthesis, Characterization, and Applications of Thiolated Silk Fibroin" (2022). WWU Graduate School Collection. 1089.
Available for download on Saturday, May 20, 2023