Stephen Boothroyd

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We have investigated the self-assembly and gelation properties of the octapeptide FEFEFKFK (F: phenylalanine; E: glutamic acid; K lysine) as a function of media pH. Temperature vs. concentration phase diagrams were constructed using the test tube tilting method at each pH. The fibre morphology and network topology formed were investigated using attenuated(More)
We investigate the possibility of using the protease thermolysin to drive the synthesis and gelation of ionic-complementary peptides from nongelling precursors. In this system, short peptide fragments are continuously interconverted to form a dynamic peptide library, which eventually favors synthesis of peptides that are thermodynamically stabilized by(More)
Oligopeptides are well-known to self-assemble into a wide array of nanostructures including β-sheet-rich fibers that when present above a critical concentration become entangled and form self-supporting hydrogels. The length, quantity, and interactions between fibers influence the mechanical properties of the hydrogel formed and this is typically achieved(More)
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