Abstract

We report the incorporation of salicylaldehyde derivatives onto the hydrazine-tagged amyloidogenic peptides by forming photoisomerizable hydrazones. These hydrazones with positive photochromism are photostable under physiological conditions and enable photoswitching without the addition of external reductants or high-power irradiation. By applying superresolution microscopy, we were able to distinguish polymorphic nanoscopic structures of the hydrazone-incorporated peptides in vitro under different buffer conditions. Moreover, the additive-free condition in our platform allows the exploration of detailed amyloid aggregate morphologies in live cells.

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