We used pH-shifting and heating to treat commercial protein isolated. The supernatants were collected and measured. The ThT assay was used to compare the formation of potential protein fibrils. It is unexpected that the commercial protein samples had the highest intensity and pH-shifting combined with heating declined this value. Does someone know the potential reasons?

Our treatment conditions:

pH-shifting: origin-12-7

Heating: boiled 30 min

Our measurement condition:

Thioflavin T: 200uM

Buffer and salt- 50 mM sodium phosphate buffer at pH 7.0