Chen B.P.-WHe R.-YChien H.-MLee C.-CChuang H.-HHsu C.-PCHUN-CHUNG CHANHuang J.J.-T.2022-04-252022-04-25202125740970https://www.scopus.com/inward/record.uri?eid=2-s2.0-85124120581&doi=10.1021%2facsanm.1c04004&partnerID=40&md5=37488d0ccb4b737a345d71f4e0843c3bhttps://scholars.lib.ntu.edu.tw/handle/123456789/606868We 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. ?acylhydrazoneamyloidfluorophorelive-cell imagingpeptide labelingphotochromicsuperresolutionGlycoproteinsImage processingNitrogen compoundsPeptidesPhotochromismAcylhydrazoneConditionHydrazonesLabelingsLive-cell imagingNano-fibrilsPeptide labelingPhotochromicsSuper resolution imagingSuperresolutionOptical resolving power[SDGs]SDG3journal article10.1021/acsanm.1c040042-s2.0-85124120581