ENZYME-MEDIATED SELF-ASSEMBLY OF HIGHLY ORDERED STRUCTURES FROM DISORDERED PROTEINS

Trypsin hydrolysis of wheat gluten produced glutamine-rich short peptides with a tendency to self-assemble into supermolecular structures extrinsic to native wheat gluten. Fourier transform infrared and X-ray diffraction data suggested that the new structures formed resembled that of cross-beta amyloid fibrils found in some insect silk and implicated in prion diseases. The superstructures were about 10 mu m in diameter with clear right-handed helical configuration and appeared to be bundles of smaller fibrils of about 63 nm in diameter. Results demonstrate the potential for utilizing cheap protein sources and natural mechanisms of protein self-assembly to design advanced nanomaterials that can provide a wide range of structural and chemical functionality.