We recorded the fluorescence spectra of experimental set 1 on a Tecan M1000pro instrument using a Greiner UV-transparent 96 well plates. The wells were filled with 140 µl of solution and the temperature was maintained constant at 25 • C. The fluorescence spectra were measured by top reading, exciting at 290 nm (5 nm bandwidth), while the emission was recorded between 300 nm and 420 nm (5 nm bandwidth). A blank spectrum (buffer) resulting from the average of 10 different spectra is subtracted before analysis. In order to determine the relative populations of soluble vs. fibrillar protein, we computed the ratios of the fluorescence intensities at 340 and 310 nm for each spectrum. We measured the fluorescence of experimental set 2, 3 and 4 in two instruments. Firstly, on a FLUOstar Omega instrument using a Hellma Analytics quartz microplate. The wells were filled with 45 µl of solution and the temperature was maintained constant at 25 • C. The fluorescence intensities were measured by top reading, exciting at 280 nm, while the emission was recorded at 310, 320, 330, 340, 350 and 360 nm (10 nm bandwidth). A blank spec-trum (buffer) is subtracted before analysis. In order to determine the relative populations of soluble vs. fibrillar protein, we computed the ratios of the fluorescence intensities at 340 and 310 nm for each spectrum. Secondly, we also measured experimental set 2, 3 and 4 in a Prometheus Panta instrument using Prometheus NT.48 Series nanoDSF high sensitivity grade capillaries. The fluorescence emission was recorded at 330 and 350 nm, exciting at 280 nm. In order to determine the relative populations of soluble vs. fibrillar protein, we computed the ratios of the fluorescence intensities at 350 and 330 nm for each spectrum, assuming an insignificant background spectrum from the buffer.