Different conditions of fibrillogenesis cause polymorphism of lysozyme amyloid fibrils

Structural differences of lysozyme amyloid fibrils prepared under different conditions were examined with the use of electron microscopy, CD spectroscopy together with a specially developed approach based on the absorption and fluorescence spectroscopy of solutions of amyloid fibrils with a specific fluorescent probe thioflavin T, prepared by equilibrium microdialysis. It was shown that the amyloid fibrils differ in their photophysical properties, morphology, parameters of thioflavin T binding. Furthermore, characteristic of the dye bound to fibrils obtained in various conditions are different. These results lead us to conclude that the conditions of fibrillogenesis can influence the rate of formation as well as the properties and structure of investigated amyloid fibrils.