Protein misfolding and aggregation have been associated with a number of hu-man diseases.As a multistep process(Fig.1a),protein unfolding yields mis-folded intermediates as either monomers or oligomers,which evolve into insolu-ble aggregates as amorphous aggregates or amyloid-β fibrils.Detection of pro-tein aggregates is of great interest as it could generate unprecedented insights into biogenesis,regulation and pathology of protein aggregation.Previous efforts using fluorescence detection have gener-ated various fluorophores with different fluorescence turn-on mechanisms and a wide spectrum coverage.However,the π-rich conjugated system of these tra-ditional fluorophores often suffers from aggregation caused quenching (ACQ).