Gelation of Misfolded Proteins

Insulin protein was exposed to mildly denaturing conditions (heat and low pH) to encourage the formation of beta-sheet rich amyloid fibrils. This resulted in an increase in viscosity of our protein samples and the morphology and thermodynamics of the resulting hydrogel were monitored using environmental scanning electron microscopy and micro differential scanning calorimetry respectively. It was found that the beta-sheet fibrils aggregated further to form macrofibrils, 2 μm in diameter and several microns in length. These long, flexible macrofibrils became entangled to form hydrogels with controllable mesh size: the higher the incubation temperature the higher the number of entanglements, and consequently the smaller the mesh size.